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bmp2  (MedChemExpress)


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    Structured Review

    MedChemExpress bmp2
    Bmp2, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/bmp2/BMP-2%2C+Human%2FMouse%2FRat/med_rxiv__64898__2026__04__07__26350283-156-38-39
    Average 94 stars, based on 5 article reviews
    bmp2 - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Blocking Assay:

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification
    Article Snippet: To conduct the Western blot analysis, the proteins in the gel were transferred to a PVDF membrane (Sigma‒ Aldrich, Germany). .. After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phosphoSmad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and antiSp7 (1:1000, MCE, China) to examine osteogenic marker expression. .. Total RNA was extracted from cells treated with recombinant proteins using a filter column kit (Vazyme, China).

    Incubation:

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification
    Article Snippet: To conduct the Western blot analysis, the proteins in the gel were transferred to a PVDF membrane (Sigma‒ Aldrich, Germany). .. After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phosphoSmad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and antiSp7 (1:1000, MCE, China) to examine osteogenic marker expression. .. Total RNA was extracted from cells treated with recombinant proteins using a filter column kit (Vazyme, China).

    Activation Assay:

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification
    Article Snippet: To conduct the Western blot analysis, the proteins in the gel were transferred to a PVDF membrane (Sigma‒ Aldrich, Germany). .. After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phosphoSmad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and antiSp7 (1:1000, MCE, China) to examine osteogenic marker expression. .. Total RNA was extracted from cells treated with recombinant proteins using a filter column kit (Vazyme, China).

    Marker:

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification
    Article Snippet: To conduct the Western blot analysis, the proteins in the gel were transferred to a PVDF membrane (Sigma‒ Aldrich, Germany). .. After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phosphoSmad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and antiSp7 (1:1000, MCE, China) to examine osteogenic marker expression. .. Total RNA was extracted from cells treated with recombinant proteins using a filter column kit (Vazyme, China).

    Expressing:

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification
    Article Snippet: To conduct the Western blot analysis, the proteins in the gel were transferred to a PVDF membrane (Sigma‒ Aldrich, Germany). .. After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phosphoSmad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and antiSp7 (1:1000, MCE, China) to examine osteogenic marker expression. .. Total RNA was extracted from cells treated with recombinant proteins using a filter column kit (Vazyme, China).

    Injection:

    Article Title: Single-Cell RNA Sequencing Identifies MMP11 + Cancer-Associated Fibroblasts as Drivers of Angiogenesis and Bladder Cancer Progression.
    Article Snippet: .. One week after tumor cell injection, the tumorbearing mice were randomly divided into four groups (n = 6 per group) and received intraperitoneal injections every two days with PBS, 2 μg kg−1 BMP2 (MedChemExpress, New Jersey, USA; HY-P7006B), 5 mg kg−1 Dorsomorphin (MedChemExpress, New Jersey, USA; HY-13418A), or a combination of the two agents. .. Tumor growthwasmonitored and recorded using a multimodal in vivo imaging system (AniView100, BioLight, Guangzhou, China) throughout the experiment.

    Article Title: Single‐Cell RNA Sequencing Identifies MMP11 + Cancer‐Associated Fibroblasts as Drivers of Angiogenesis and Bladder Cancer Progression
    Article Snippet: .. One week after tumor cell injection, the tumor‐bearing mice were randomly divided into four groups ( n = 6 per group) and received intraperitoneal injections every two days with PBS, 2 μg kg −1 BMP2 (MedChemExpress, New Jersey, USA; HY‐P7006B), 5 mg kg −1 Dorsomorphin (MedChemExpress, New Jersey, USA; HY‐13418A), or a combination of the two agents. .. Tumor growth was monitored and recorded using a multimodal in vivo imaging system (AniView100, BioLight, Guangzhou, China) throughout the experiment.

    Transduction:

    Article Title: Nonsense suppression induces read-through of a novel BMPR1A variant in a Chinese family with hereditary colorectal cancer.
    Article Snippet: Funding information National Natural Science Foundation of China, Grant/Award Number: 81773159 Abstract Background: BMPR1A-mediated signaling transduction plays an essential role in intestinal growth.. Variations of BMPR1A lead to a rare autosomal dominant inherited juvenile polyposis syndrome (JPS) with high probability of developing into colorectal cancer (CRC).. Nonsense and frameshift variations, generating premature termination codons (PTCs), are the most pathogenic variants in the BMPR1A gene.



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    Image Search Results


    Intracellular bacteria impair BMSCs osteogenesis despite antibiotic treatment. (A) Micro-CT analysis showing 3D overview and 2D cross-sectional views of femoral bones from the indicated experimental groups at 30 days post-intervention. (B) Bone-related parameters, including bone mineral density (BMD), bone volume/total volume (BV/TV), trabecular separation (Tb.Sp), trabecular thickness (Tb.Th), cortical porosity (Ct.Po), and trabecular number (Tb.N), were quantified (n = 6). (C, D) Immunofluorescence staining of BMP-2 in the femoral bone tissues of mice, with subsequent quantification (original magnification ×63; scale bar = 50 µm). (E, F) Immunofluorescence staining of Runx-2 in the femoral bones, along with quantitative analysis. (G) Histological analysis of bone tissue sections stained for bacteria in the control, bacterial, and antibiotic-treated groups. Cell nuclei are stained blue with DAPI, cell membranes are stained green with wheat germ agglutinin, and S. aureus is stained red. In the merged image, triangles indicate intracellular bacteria, while pentagrams denote extracellular bacteria. (H) Quantitative assessment of intracellular and extracellular bacteria and their corresponding MOI.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: Intracellular bacteria impair BMSCs osteogenesis despite antibiotic treatment. (A) Micro-CT analysis showing 3D overview and 2D cross-sectional views of femoral bones from the indicated experimental groups at 30 days post-intervention. (B) Bone-related parameters, including bone mineral density (BMD), bone volume/total volume (BV/TV), trabecular separation (Tb.Sp), trabecular thickness (Tb.Th), cortical porosity (Ct.Po), and trabecular number (Tb.N), were quantified (n = 6). (C, D) Immunofluorescence staining of BMP-2 in the femoral bone tissues of mice, with subsequent quantification (original magnification ×63; scale bar = 50 µm). (E, F) Immunofluorescence staining of Runx-2 in the femoral bones, along with quantitative analysis. (G) Histological analysis of bone tissue sections stained for bacteria in the control, bacterial, and antibiotic-treated groups. Cell nuclei are stained blue with DAPI, cell membranes are stained green with wheat germ agglutinin, and S. aureus is stained red. In the merged image, triangles indicate intracellular bacteria, while pentagrams denote extracellular bacteria. (H) Quantitative assessment of intracellular and extracellular bacteria and their corresponding MOI.

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Bacteria, Micro-CT, Immunofluorescence, Staining, Control

    Transcriptome sequencing demonstrated increased global phosphorylation. (A, B) Live/dead cell staining and quantification following bacterial infection at different MOIs (100, 200, 400) and time points (2 h, 4 h) (scale bar = 50 µm; n = 3). (C, D) ALP staining and fluorescence intensity quantification before and after bacterial infection. (E) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in control and bacteria groups. (F, G) Western blotting and corresponding quantitative analysis of BMP-2, Runx-2, Alp and Collagen I in control and bacteria groups. (H) Volcano plot of transcriptome sequencing differential expression between the control group and bacteria-infected group [Dashed box: phosphorylation-related genes (Top10)]. (I) Heatmap of differential gene expression. (J) Top 20 keggenriched gene pathways based on transcriptome sequencing between the control group and bacteria-infected group (Red font: Extracellular matrix and adhesion-related pathways). (K) GSEA plot of the focal adhesion signaling pathway. (L, M) Western blot analysis and quantitative measurement of Fak protein expression in the control and bacteria-infected groups (n = 3). (N, O) Western blot analysis and quantitative measurement of global phosphotyrosine levels in the control and bacteria-infected groups. (P, Q) Western blot analysis and quantitative measurement of global phosphoserine/threonine levels in the control and bacteria-infected groups.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: Transcriptome sequencing demonstrated increased global phosphorylation. (A, B) Live/dead cell staining and quantification following bacterial infection at different MOIs (100, 200, 400) and time points (2 h, 4 h) (scale bar = 50 µm; n = 3). (C, D) ALP staining and fluorescence intensity quantification before and after bacterial infection. (E) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in control and bacteria groups. (F, G) Western blotting and corresponding quantitative analysis of BMP-2, Runx-2, Alp and Collagen I in control and bacteria groups. (H) Volcano plot of transcriptome sequencing differential expression between the control group and bacteria-infected group [Dashed box: phosphorylation-related genes (Top10)]. (I) Heatmap of differential gene expression. (J) Top 20 keggenriched gene pathways based on transcriptome sequencing between the control group and bacteria-infected group (Red font: Extracellular matrix and adhesion-related pathways). (K) GSEA plot of the focal adhesion signaling pathway. (L, M) Western blot analysis and quantitative measurement of Fak protein expression in the control and bacteria-infected groups (n = 3). (N, O) Western blot analysis and quantitative measurement of global phosphotyrosine levels in the control and bacteria-infected groups. (P, Q) Western blot analysis and quantitative measurement of global phosphoserine/threonine levels in the control and bacteria-infected groups.

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Sequencing, Phospho-proteomics, Staining, Infection, Fluorescence, Quantitative RT-PCR, Expressing, Control, Bacteria, Western Blot, Quantitative Proteomics, Gene Expression

    Integrated omics reveals talin-1 as key for bacterial internalization. (A) PCA analysis of proteomics and phosphoproteomics. (B) Top 20 significantly enriched go pathways shared (Red font: extracellular matrix and adhesion-related pathways). (C) Volcano plot of proteomics data (No significant difference in Talin-1 protein expression). (D) Volcano plot of phosphoproteomics data (all significantly altered Talin-1 modification sites are up-regulated). (E, F) Western blotting and quantitative analysis of Talin-1 transfection experiments. (G, H) Comparison of intracellular colony formation at 1/3/7 days: si-Talin vs. Bacterial groups (n = 3). (I, J) ALP fluorescence staining and quantitative analysis of fluorescence intensity at 1/3/7 days between si-Talin and bacterial groups. (K) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in control, bacteria and si-Talin-1 groups. (L, M) Western blotting and corresponding quantitative analysis of BMP-2, Runx-2, Alp and Collagen I in control, bacteria, and si-Talin-1 groups.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: Integrated omics reveals talin-1 as key for bacterial internalization. (A) PCA analysis of proteomics and phosphoproteomics. (B) Top 20 significantly enriched go pathways shared (Red font: extracellular matrix and adhesion-related pathways). (C) Volcano plot of proteomics data (No significant difference in Talin-1 protein expression). (D) Volcano plot of phosphoproteomics data (all significantly altered Talin-1 modification sites are up-regulated). (E, F) Western blotting and quantitative analysis of Talin-1 transfection experiments. (G, H) Comparison of intracellular colony formation at 1/3/7 days: si-Talin vs. Bacterial groups (n = 3). (I, J) ALP fluorescence staining and quantitative analysis of fluorescence intensity at 1/3/7 days between si-Talin and bacterial groups. (K) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in control, bacteria and si-Talin-1 groups. (L, M) Western blotting and corresponding quantitative analysis of BMP-2, Runx-2, Alp and Collagen I in control, bacteria, and si-Talin-1 groups.

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Phospho-proteomics, Expressing, Modification, Western Blot, Transfection, Comparison, Fluorescence, Staining, Quantitative RT-PCR, Control, Bacteria

    Mprip physically interacts with Talin-1 to trigger its subsequent phosphorylation. (A) Ranked list of Talin-1 interacting proteins. (B) Confocal fluorescence images showing colocalization of host Mprip and Talin-1 upon S. aureus infection. Blue indicates DAPI; green, Mprip protein; red, Talin-1 protein. (scale bar = 50 µm). (C) Co-IP assay demonstrating the interaction between Talin and Mprip. (D) Transfection efficiency of siRNA targeting Mprip (si-Mprip). (E) Quantitative analysis of si-Mprip transfection (n = 3). (F, G) Western blot analysis showing that knockdown of Mprip decreases the protein expression level of phosphorylated Talin. (H) RT-qPCR analysis of osteogenic markers BMP-2, Runx-2, Alp, and Collagen I in control, bacterial, and si-Mprip groups. (I, J) Western blot analysis and quantification of BMP-2, Runx-2, Alp, and Collagen I expression in control, bacterial, and si-Mprip groups (n = 3).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: Mprip physically interacts with Talin-1 to trigger its subsequent phosphorylation. (A) Ranked list of Talin-1 interacting proteins. (B) Confocal fluorescence images showing colocalization of host Mprip and Talin-1 upon S. aureus infection. Blue indicates DAPI; green, Mprip protein; red, Talin-1 protein. (scale bar = 50 µm). (C) Co-IP assay demonstrating the interaction between Talin and Mprip. (D) Transfection efficiency of siRNA targeting Mprip (si-Mprip). (E) Quantitative analysis of si-Mprip transfection (n = 3). (F, G) Western blot analysis showing that knockdown of Mprip decreases the protein expression level of phosphorylated Talin. (H) RT-qPCR analysis of osteogenic markers BMP-2, Runx-2, Alp, and Collagen I in control, bacterial, and si-Mprip groups. (I, J) Western blot analysis and quantification of BMP-2, Runx-2, Alp, and Collagen I expression in control, bacterial, and si-Mprip groups (n = 3).

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Phospho-proteomics, Fluorescence, Infection, Co-Immunoprecipitation Assay, Transfection, Western Blot, Knockdown, Expressing, Quantitative RT-PCR, Control

    Talin-1 inhibits osteogenesis by activating the PI3K-AKT pathway. (A, B) Western blot analysis and quantitative comparison of PI3K–AKT activator (740 Y-P at a concentration of 20 μM) and inhibitor (PI3K/AKT-IN-1 (2.62 µM)) treatments. (C, D) Western blot analysis and quantitative measurement of PI3K/p-PI3K and AKT/p-AKT in Control, Bacteria, and Bacteria + si-Talin-1 groups. (E) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in Control, Bacteria, and Bacteria + PI3K (-) groups, PI3K (-): PI3K/AKT pathway inhibitor. (F, G) Western blot analysis and quantification of BMP-2, Runx-2, Alp, and Collagen I in Control, Bacteria, and Bacteria + PI3K (-) groups. (H) RT-qPCR analysis of BMP-2 and Runx-2 in Control, Bacteria, Bacteria + si-Talin-1, and Bacteria + si-Talin-1 + PI3K(+) groups. (I, J) Western blot analysis and quantitative assessment of BMP-2 and Runx-2 in Control, Bacteria, Bacteria + si-Talin-1, and Bacteria + si-Talin-1 + PI3K (+) groups (n = 3).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: Talin-1 inhibits osteogenesis by activating the PI3K-AKT pathway. (A, B) Western blot analysis and quantitative comparison of PI3K–AKT activator (740 Y-P at a concentration of 20 μM) and inhibitor (PI3K/AKT-IN-1 (2.62 µM)) treatments. (C, D) Western blot analysis and quantitative measurement of PI3K/p-PI3K and AKT/p-AKT in Control, Bacteria, and Bacteria + si-Talin-1 groups. (E) RT-qPCR analysis of BMP-2, Runx-2, Alp, and Collagen I expression in Control, Bacteria, and Bacteria + PI3K (-) groups, PI3K (-): PI3K/AKT pathway inhibitor. (F, G) Western blot analysis and quantification of BMP-2, Runx-2, Alp, and Collagen I in Control, Bacteria, and Bacteria + PI3K (-) groups. (H) RT-qPCR analysis of BMP-2 and Runx-2 in Control, Bacteria, Bacteria + si-Talin-1, and Bacteria + si-Talin-1 + PI3K(+) groups. (I, J) Western blot analysis and quantitative assessment of BMP-2 and Runx-2 in Control, Bacteria, Bacteria + si-Talin-1, and Bacteria + si-Talin-1 + PI3K (+) groups (n = 3).

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Western Blot, Comparison, Concentration Assay, Control, Bacteria, Quantitative RT-PCR, Expressing

    UM-164 blocks bacterial internalization and promotes bone formation by inhibiting talin-1 phosphorylation. (A) Virtual screening of small-molecule compounds binding to Talin-1. (B) Molecular docking simulation of UM-164 with Talin-1. (C) SPR assay evaluating the interaction (KD: dissociation constant, which reflects the affinity of the analyte to the target. The smaller the value, the stronger the affinity; Ka: association rate constant, which represents the speed of intermolecular binding. The larger the value, the faster the binding; Kd: dissociation rate constant, which represents the speed of intermolecular dissociation. The larger the value, the faster the dissociation). (D) CCK-8 cell viability assay performed on cells treated with UM-164 at concentrations of 0, 0.001, 0.01, 0.1, 1 and 10 μM. Cell viability decreased significantly as the concentration increased from 0.1 μM to 1 μM. (E) UM-164 treatment decreased the binding affinity between talin-1 and Mprip, as revealed by Co-IP assay. (F, G) Western blot analysis showing that UM-164 treatment decreases the phosphorylation level of Talin-1. (H, I) Intracellular bacterial CFU assays and statistical analysis comparing untreated and UM-164-treated cells (0.1 μM; labeled as “UM-164” in panel I) at 1/3/7 days post-infection. (J, K) RT-qPCR analysis of BMP-2 and Runx-2 expression levels following treatment with different concentrations of UM-164 (0, 0.001, 0.01, 0.1, 1 and 10 μM). (L–N) Western blotting and quantitative analysis of BMP-2 and Runx-2 protein levels after treatment with varying concentrations of UM-164 (0, 0.001, 0.01, 0.1, 1and 10 μM) (n = 3).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: UM-164 blocks bacterial internalization and promotes bone formation by inhibiting talin-1 phosphorylation. (A) Virtual screening of small-molecule compounds binding to Talin-1. (B) Molecular docking simulation of UM-164 with Talin-1. (C) SPR assay evaluating the interaction (KD: dissociation constant, which reflects the affinity of the analyte to the target. The smaller the value, the stronger the affinity; Ka: association rate constant, which represents the speed of intermolecular binding. The larger the value, the faster the binding; Kd: dissociation rate constant, which represents the speed of intermolecular dissociation. The larger the value, the faster the dissociation). (D) CCK-8 cell viability assay performed on cells treated with UM-164 at concentrations of 0, 0.001, 0.01, 0.1, 1 and 10 μM. Cell viability decreased significantly as the concentration increased from 0.1 μM to 1 μM. (E) UM-164 treatment decreased the binding affinity between talin-1 and Mprip, as revealed by Co-IP assay. (F, G) Western blot analysis showing that UM-164 treatment decreases the phosphorylation level of Talin-1. (H, I) Intracellular bacterial CFU assays and statistical analysis comparing untreated and UM-164-treated cells (0.1 μM; labeled as “UM-164” in panel I) at 1/3/7 days post-infection. (J, K) RT-qPCR analysis of BMP-2 and Runx-2 expression levels following treatment with different concentrations of UM-164 (0, 0.001, 0.01, 0.1, 1 and 10 μM). (L–N) Western blotting and quantitative analysis of BMP-2 and Runx-2 protein levels after treatment with varying concentrations of UM-164 (0, 0.001, 0.01, 0.1, 1and 10 μM) (n = 3).

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: Phospho-proteomics, Binding Assay, SPR Assay, CCK-8 Assay, Viability Assay, Concentration Assay, Co-Immunoprecipitation Assay, Western Blot, Labeling, Infection, Quantitative RT-PCR, Expressing

    UM-164 blocks bacterial uptake and restores bone formation in vivo . (A) Micro-CT imaging of femurs from the four experimental groups: control, bacterial infection, antibiotic treatment, and antibiotic + drug treatment. (B) quantitative analysis of micro-CT derived trabecular and cortical bone parameters: BMD, BV/TV, Tb.Sp, Tb.Th, Ct.Po, and Tb.N. (C, D) Immunofluorescence staining of BMP-2 in the femur, along with quantitative analysis (original magnification ×63; scale bar = 50 µm; n = 6). (E, F) Immunofluorescence staining of Runx-2 in the femur, along with quantitative analysis. (G) Histological staining of S. aureus in the femurs of mice across different groups: normal, bacterial infection, antibiotic treatment, and antibiotic + UM-164 treatment. (H) Quantitative analysis of intra- and extracellular bacterial loads, as well as intra- and extracellular bacteria-to-host cell ratios.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Enhancement of antibiotic therapy in osteomyelitis by inhibiting talin-1-mediated bacterial internalization

    doi: 10.3389/fcimb.2026.1823065

    Figure Lengend Snippet: UM-164 blocks bacterial uptake and restores bone formation in vivo . (A) Micro-CT imaging of femurs from the four experimental groups: control, bacterial infection, antibiotic treatment, and antibiotic + drug treatment. (B) quantitative analysis of micro-CT derived trabecular and cortical bone parameters: BMD, BV/TV, Tb.Sp, Tb.Th, Ct.Po, and Tb.N. (C, D) Immunofluorescence staining of BMP-2 in the femur, along with quantitative analysis (original magnification ×63; scale bar = 50 µm; n = 6). (E, F) Immunofluorescence staining of Runx-2 in the femur, along with quantitative analysis. (G) Histological staining of S. aureus in the femurs of mice across different groups: normal, bacterial infection, antibiotic treatment, and antibiotic + UM-164 treatment. (H) Quantitative analysis of intra- and extracellular bacterial loads, as well as intra- and extracellular bacteria-to-host cell ratios.

    Article Snippet: Antibodies used: BMP-2 (A0231, ABclonal, China), Runx-2 (A11753, ABclonal, China), Alp (A0514, ABclonal, China), Collagen-1 (A21059, ABclonal, China), Talin-1 (14168-1-AP, Proteintech, China), FAK (66258-1-Ig, Proteintech, China), Pan phospho-Serine/Threonine Mouse mAb (AP1067, ABclonal, China), Pan phospho-Tyrosine Mouse mAb (AP0973, ABclonal, China), Mprip (D8G8R, Cell Signaling Technology, USA).

    Techniques: In Vivo, Micro-CT, Imaging, Control, Infection, Derivative Assay, Immunofluorescence, Staining, Bacteria

    Preparation of the D-Bmp2@M system and its therapeutic mechanism for osteoporosis fractures. Bmp2 fused with DSS6 were expressed in HEK293T and then encapsulated in porous PLGA microspheres to construct the D-Bmp2@M system. Upon injection into the osteoporotic fracture site, the system gradually releases D-Bmp2 as the microspheres degrade over approximately 30 days. The released D-Bmp2 actively binds to bone tissue due to the affinity of DSS6 for bone. This localized enrichment promotes osteogenic activity at the fracture site, promoting fracture healing while reducing the risk of ectopic bone formation. The sustained-release and targeted delivery systems provides a superior therapeutic strategy for fracture treatment.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: Preparation of the D-Bmp2@M system and its therapeutic mechanism for osteoporosis fractures. Bmp2 fused with DSS6 were expressed in HEK293T and then encapsulated in porous PLGA microspheres to construct the D-Bmp2@M system. Upon injection into the osteoporotic fracture site, the system gradually releases D-Bmp2 as the microspheres degrade over approximately 30 days. The released D-Bmp2 actively binds to bone tissue due to the affinity of DSS6 for bone. This localized enrichment promotes osteogenic activity at the fracture site, promoting fracture healing while reducing the risk of ectopic bone formation. The sustained-release and targeted delivery systems provides a superior therapeutic strategy for fracture treatment.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: Construct, Injection, Activity Assay

    Design and validation of bone-targeted Bmp2. a. Schematic representation of the Bmp2/D-Bmp2 plasmid constructs and the structure predicted by AlphaFold3. b. Immunofluorescence staining of HEK-293T cells transfected with the plasmids: phalloidin (green), DAPI (blue), and Alexa Fluor 647-conjugated anti-Flag antibodies (red). Scale bar: 10 μm. c. SDS-PAGE of purified proteins. d. Western blot validation of protein expression. e. Bmp2 activity reporter assay: schematic of the luciferase reporter system (left), representative fluorescence images, and statistical analysis of firefly luciferase activity by in vivo imaging system (IVIS) (a.u.: arbitrary units) (right, n = 3 per group). f. qPCR analysis of Bmp2 signaling pathway-related mRNA levels in MC3T3-E1 cells treated with the Bmp2 or D-Bmp2 protein (n = 3 per group). g, h. Western blot (g) and quantification of Bmp2 pathway-related protein expression in treated MC3T3-E1 cells (h) (n = 3 per group). i. Schematic of the HA-coated ELISA plate and HA-binding affinity assay (n = 3 per group). j. Tissue-specific binding assay of Bmp2 or D-Bmp2: Mouse muscle slices (left, scale bar: 100 μm) and undecalcified femur slices (right, scale bar: 200 μm) stained with AF647-conjugated anti-Flag antibodies. The data are presented as the means ± standard deviations (SDs). One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: Design and validation of bone-targeted Bmp2. a. Schematic representation of the Bmp2/D-Bmp2 plasmid constructs and the structure predicted by AlphaFold3. b. Immunofluorescence staining of HEK-293T cells transfected with the plasmids: phalloidin (green), DAPI (blue), and Alexa Fluor 647-conjugated anti-Flag antibodies (red). Scale bar: 10 μm. c. SDS-PAGE of purified proteins. d. Western blot validation of protein expression. e. Bmp2 activity reporter assay: schematic of the luciferase reporter system (left), representative fluorescence images, and statistical analysis of firefly luciferase activity by in vivo imaging system (IVIS) (a.u.: arbitrary units) (right, n = 3 per group). f. qPCR analysis of Bmp2 signaling pathway-related mRNA levels in MC3T3-E1 cells treated with the Bmp2 or D-Bmp2 protein (n = 3 per group). g, h. Western blot (g) and quantification of Bmp2 pathway-related protein expression in treated MC3T3-E1 cells (h) (n = 3 per group). i. Schematic of the HA-coated ELISA plate and HA-binding affinity assay (n = 3 per group). j. Tissue-specific binding assay of Bmp2 or D-Bmp2: Mouse muscle slices (left, scale bar: 100 μm) and undecalcified femur slices (right, scale bar: 200 μm) stained with AF647-conjugated anti-Flag antibodies. The data are presented as the means ± standard deviations (SDs). One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: Biomarker Discovery, Plasmid Preparation, Construct, Immunofluorescence, Staining, Transfection, SDS Page, Purification, Western Blot, Expressing, Activity Assay, Reporter Assay, Luciferase, Fluorescence, In Vivo Imaging, Enzyme-linked Immunosorbent Assay, Binding Assay

    Preparation and characterization of self-healing sustained-release microspheres loaded with D-Bmp2. a. Representative SEM images of microspheres before (top) and after (bottom) healing; left scale bar: 10 μm; middle and right scale bar: 2.5 μm. b. Statistical analysis of the microsphere diameter before and after healing determined via SEM. c. Representative confocal microscopy images of protein-loaded microspheres: PLGA microspheres (red) and Cy5-labeled D-Bmp2 (blue). Scale bar: 2 μm. d. Morphology of lyophilized D-Bmp2@M powder. e. SDS-PAGE of lyophilized D-Bmp2@M powder at different storage times. f. Representative firefly luciferase images from bioactivity assays of lyophilized D-Bmp2@M powder at different times. g. Activity change curve of lyophilized D-Bmp2@M powder at different time points (n = 3 per group). h, i. In vitro fluorescence intensity changes of Cy7-labeled D-Bmp2 from microspheres: (h) Representative fluorescence images of Cy7-D-Bmp2 maintained in microspheres (0–30 days) (top) and representative SEM images of microsphere degradation at different time points. Scale bar: 2.5 μm (bottom); (i) Relative fluorescence intensity change of Cy7-D-Bmp2 maintained in microspheres (n = 3 per group). j. Representative firefly luciferase images from Bmp2 reporter assays. k. Protein activity normalization: ratio of luminescence intensity (data from ) to protein concentration (data from ) (n = 3 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant).

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: Preparation and characterization of self-healing sustained-release microspheres loaded with D-Bmp2. a. Representative SEM images of microspheres before (top) and after (bottom) healing; left scale bar: 10 μm; middle and right scale bar: 2.5 μm. b. Statistical analysis of the microsphere diameter before and after healing determined via SEM. c. Representative confocal microscopy images of protein-loaded microspheres: PLGA microspheres (red) and Cy5-labeled D-Bmp2 (blue). Scale bar: 2 μm. d. Morphology of lyophilized D-Bmp2@M powder. e. SDS-PAGE of lyophilized D-Bmp2@M powder at different storage times. f. Representative firefly luciferase images from bioactivity assays of lyophilized D-Bmp2@M powder at different times. g. Activity change curve of lyophilized D-Bmp2@M powder at different time points (n = 3 per group). h, i. In vitro fluorescence intensity changes of Cy7-labeled D-Bmp2 from microspheres: (h) Representative fluorescence images of Cy7-D-Bmp2 maintained in microspheres (0–30 days) (top) and representative SEM images of microsphere degradation at different time points. Scale bar: 2.5 μm (bottom); (i) Relative fluorescence intensity change of Cy7-D-Bmp2 maintained in microspheres (n = 3 per group). j. Representative firefly luciferase images from Bmp2 reporter assays. k. Protein activity normalization: ratio of luminescence intensity (data from ) to protein concentration (data from ) (n = 3 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant).

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: Confocal Microscopy, Labeling, SDS Page, Luciferase, Activity Assay, In Vitro, Fluorescence, Protein Concentration

    In vitro validation of D-Bmp2@M osteogenic efficacy and inhibition of ectopic ossification. a. Schematic diagram of the osteoblast-bone Transwell model. Bmp2/D-Bmp2@M microspheres or free Bmp2/D-Bmp2 were loaded in the upper chambers, MC3T3-E1 cells were cultured on two coverslips (one of which was precoated with HA) in the lower compartments, and the medium was refreshed every day for 7 or 14 days. Alkaline phosphatase (ALP) and Alizarin Red S (ARS) staining were performed at days 7 and 14, respectively. b. Osteogenic differentiation staining: ALP (early-stage, day 7) and ARS (late-stage, day 14) staining. Scale bar: 200 μm. c. ALP activity was quantitatively analyzed using an ALP kit (n = 3 per group). d. Relative quantitative analysis of ARS staining was performed at an OD of 562 nm (n = 3 per group). e. qPCR analysis of Bmp2 signaling-related mRNA in MC3T3-E1 cells (n = 3 per group). f. Schematic diagram of the muscle-bone Transwell model. Bovine bone slices were co-incubated with Bmp2/D-Bmp2@M or free Bmp2/D-Bmp2 in the upper chambers, and C2C12 cells were cultured in the lower chambers and the medium was refreshed every day for 7 days. D-Bmp2 and Bmp2 retention on bone slices and ALP staining of C2C12 cells were analyzed on day 7. g. Representative fluorescence imaging of bone slices incubated with AF647-conjugated anti-Flag antibodies (above) (yellow arrows: bone slice) and C2C12 ALP staining images (below), scale bar: 200 μm. h. AF647-conjugated anti-Flag antibody fluorescence intensity quantification in bone slices (n = 3 per group). i. Quantification of ALP activity in C2C12 cells (n = 3 per group). j. qPCR analysis of Bmp2 signaling-related mRNA in C2C12 cells (n = 3 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗ p < 0.05, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: In vitro validation of D-Bmp2@M osteogenic efficacy and inhibition of ectopic ossification. a. Schematic diagram of the osteoblast-bone Transwell model. Bmp2/D-Bmp2@M microspheres or free Bmp2/D-Bmp2 were loaded in the upper chambers, MC3T3-E1 cells were cultured on two coverslips (one of which was precoated with HA) in the lower compartments, and the medium was refreshed every day for 7 or 14 days. Alkaline phosphatase (ALP) and Alizarin Red S (ARS) staining were performed at days 7 and 14, respectively. b. Osteogenic differentiation staining: ALP (early-stage, day 7) and ARS (late-stage, day 14) staining. Scale bar: 200 μm. c. ALP activity was quantitatively analyzed using an ALP kit (n = 3 per group). d. Relative quantitative analysis of ARS staining was performed at an OD of 562 nm (n = 3 per group). e. qPCR analysis of Bmp2 signaling-related mRNA in MC3T3-E1 cells (n = 3 per group). f. Schematic diagram of the muscle-bone Transwell model. Bovine bone slices were co-incubated with Bmp2/D-Bmp2@M or free Bmp2/D-Bmp2 in the upper chambers, and C2C12 cells were cultured in the lower chambers and the medium was refreshed every day for 7 days. D-Bmp2 and Bmp2 retention on bone slices and ALP staining of C2C12 cells were analyzed on day 7. g. Representative fluorescence imaging of bone slices incubated with AF647-conjugated anti-Flag antibodies (above) (yellow arrows: bone slice) and C2C12 ALP staining images (below), scale bar: 200 μm. h. AF647-conjugated anti-Flag antibody fluorescence intensity quantification in bone slices (n = 3 per group). i. Quantification of ALP activity in C2C12 cells (n = 3 per group). j. qPCR analysis of Bmp2 signaling-related mRNA in C2C12 cells (n = 3 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗ p < 0.05, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: In Vitro, Biomarker Discovery, Inhibition, Cell Culture, Staining, Activity Assay, Incubation, Fluorescence, Imaging

    In vivo testing of release kinetics and bone accumulation of D-Bmp2@M. a. Representative fluorescence images showing the changes in Cy7 fluorescence after local injection. b. Quantitative analysis of the changes in relative fluorescence intensity (n = 6 per group). c. Representative ex vivo fluorescence images of bone tissues at 1 day post-injection of free Cy7-D-Bmp2 or Cy7-Bmp2, along with quantitative analysis of the bone fluorescence intensity (n = 6 per group). d. Representative IFHC images at 1 day post-injection showing Bmp2 or D-Bmp2 localization and the bone to muscle fluorescence intensity ratio (n = 6 per group). IFHC: anti-Flag antibody (yellow), DAPI (blue); the white dotted line represents the boundary between bones and muscles (M: muscle, B: bone); scale bar: 20 μm. e. Representative ex vivo fluorescence images of bone tissues at 6 days post-injection of PLGA microspheres loaded with Cy7-D-Bmp2 or Cy7-Bmp2, along with quantitative analysis of the bone fluorescence intensity (n = 6 per group). f. Representative IFHC images at 6 days post-injection showing Bmp2 or D-Bmp2 localization and the bone-to-muscle fluorescence intensity ratio (the fluorescence intensity of the 10-μm bone boundary to muscle tissue) (n = 6 per group). IFHC: anti-Flag antibody (yellow), DAPI (blue); the white arrows highlight PLGA microspheres; the white dotted line represents the boundary between bones and muscles (M: muscle, B: bone); scale bar: 20 μm. The data are presented as the means ± standard deviations (SDs). Unpaired Student's t -test was used for two-group comparisons. Significance levels: ∗∗∗∗ p < 0.0001.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: In vivo testing of release kinetics and bone accumulation of D-Bmp2@M. a. Representative fluorescence images showing the changes in Cy7 fluorescence after local injection. b. Quantitative analysis of the changes in relative fluorescence intensity (n = 6 per group). c. Representative ex vivo fluorescence images of bone tissues at 1 day post-injection of free Cy7-D-Bmp2 or Cy7-Bmp2, along with quantitative analysis of the bone fluorescence intensity (n = 6 per group). d. Representative IFHC images at 1 day post-injection showing Bmp2 or D-Bmp2 localization and the bone to muscle fluorescence intensity ratio (n = 6 per group). IFHC: anti-Flag antibody (yellow), DAPI (blue); the white dotted line represents the boundary between bones and muscles (M: muscle, B: bone); scale bar: 20 μm. e. Representative ex vivo fluorescence images of bone tissues at 6 days post-injection of PLGA microspheres loaded with Cy7-D-Bmp2 or Cy7-Bmp2, along with quantitative analysis of the bone fluorescence intensity (n = 6 per group). f. Representative IFHC images at 6 days post-injection showing Bmp2 or D-Bmp2 localization and the bone-to-muscle fluorescence intensity ratio (the fluorescence intensity of the 10-μm bone boundary to muscle tissue) (n = 6 per group). IFHC: anti-Flag antibody (yellow), DAPI (blue); the white arrows highlight PLGA microspheres; the white dotted line represents the boundary between bones and muscles (M: muscle, B: bone); scale bar: 20 μm. The data are presented as the means ± standard deviations (SDs). Unpaired Student's t -test was used for two-group comparisons. Significance levels: ∗∗∗∗ p < 0.0001.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: In Vivo, Fluorescence, Injection, Ex Vivo, Muscles

    D-Bmp2@M accelerates fracture healing in mice and reduces ectopic osteogenesis. a. Schematic of the fracture treatment procedure: C57BL/6 mice underwent transverse femoral fracture induction followed by 28-day treatment. b. Representative X-ray images of the fracture healing process at different time points: white arrows (fracture location), red arrows (early callus), blue dotted lines (femur boundary), yellow dotted lines (callus boundary), and yellow arrows (ectopic ossification). Scale bar: 5 mm. c. Micro-CT 3D reconstruction of femurs on day 28 post-treatment; yellow arrows highlight heterotopic ossification; COR (coronal), SAG (sagittal), and TRA (transverse) Scale bar: 1 mm. d-g. Micro-CT quantitative analysis: (d) BMD, (e) BV, (f) TV, and (g) the BV/TV ratio of the fracture callus (n = 6 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: D-Bmp2@M accelerates fracture healing in mice and reduces ectopic osteogenesis. a. Schematic of the fracture treatment procedure: C57BL/6 mice underwent transverse femoral fracture induction followed by 28-day treatment. b. Representative X-ray images of the fracture healing process at different time points: white arrows (fracture location), red arrows (early callus), blue dotted lines (femur boundary), yellow dotted lines (callus boundary), and yellow arrows (ectopic ossification). Scale bar: 5 mm. c. Micro-CT 3D reconstruction of femurs on day 28 post-treatment; yellow arrows highlight heterotopic ossification; COR (coronal), SAG (sagittal), and TRA (transverse) Scale bar: 1 mm. d-g. Micro-CT quantitative analysis: (d) BMD, (e) BV, (f) TV, and (g) the BV/TV ratio of the fracture callus (n = 6 per group). The data are presented as the means ± SDs. One-way ANOVA was used for multiple comparisons. Significance levels: ns (not significant), ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗∗ p < 0.0001.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: Micro-CT

    D-Bmp2@M accelerates fracture healing in osteoporotic mice. a. Schematic of the osteoporotic fracture treatment procedure: C57BL/6 mice underwent bilateral ovariectomy (OVX) to establish an osteoporosis model, followed by transverse femoral fracture induction and 28 days of treatment. b. Representative X-ray images of the fracture healing process at different time points and Micro-CT 3D reconstruction of femurs on day 28 post-treatment: white arrows (fracture location), red arrows (early callus), blue dotted lines (femur boundary), and yellow dashed lines (callus boundary). Scale bar of x-ray: 5 mm; Scale bar of 3D reconstruction: 1 mm. c. Quantitative analysis of the fracture callus BMD and BV/TV (normal PBS Ctrl group data from PBS group in d–g) (n = 6 per group). d. Representative H&E staining images and representative Masson's trichrome staining images of fracture calluses at 28 days. Scale bar: 50 μm. e. Quantification of the callus area/total bone area ratio and quantification of the new bone area/total bone area ratio (n = 6 per group). f, g. Representative IFHC images of the callus region at 28 days and quantification of the relative fluorescence intensities: (f) The white dotted line represents the boundary between the callus and muscles (M: muscle, C: callus); Runx2 (red), ALP (green), and DAPI (blue). Scale bar: 50 μm; (g) Quantification of the relative fluorescence intensities of Runx2 and ALP (n = 6 per group). h, i. Representative IFHC images of the callus region at 28 days and quantification of the relative fluorescence intensities: (h) The white dotted line represents the boundary between the callus and muscles (M: muscle, C: callus); Sp7 (red), ALP (green), and DAPI (blue). Scale bar: 50 μm; (i) Quantification of the relative fluorescence intensities of Sp7 and ALP (n = 6 per group). The data are presented as the means ± standard deviations (SDs). Unpaired Student's t -test was used for two-group comparisons. One-way ANOVA was used for multiple comparisons. Significance levels: ∗ p < 0.05, ∗∗∗∗ p < 0.0001.

    Journal: Bioactive Materials

    Article Title: Sustained release PLGA microspheres loaded with a bone-affinity Bmp2 enhance fracture healing and mitigate heterotopic ossification

    doi: 10.1016/j.bioactmat.2026.02.050

    Figure Lengend Snippet: D-Bmp2@M accelerates fracture healing in osteoporotic mice. a. Schematic of the osteoporotic fracture treatment procedure: C57BL/6 mice underwent bilateral ovariectomy (OVX) to establish an osteoporosis model, followed by transverse femoral fracture induction and 28 days of treatment. b. Representative X-ray images of the fracture healing process at different time points and Micro-CT 3D reconstruction of femurs on day 28 post-treatment: white arrows (fracture location), red arrows (early callus), blue dotted lines (femur boundary), and yellow dashed lines (callus boundary). Scale bar of x-ray: 5 mm; Scale bar of 3D reconstruction: 1 mm. c. Quantitative analysis of the fracture callus BMD and BV/TV (normal PBS Ctrl group data from PBS group in d–g) (n = 6 per group). d. Representative H&E staining images and representative Masson's trichrome staining images of fracture calluses at 28 days. Scale bar: 50 μm. e. Quantification of the callus area/total bone area ratio and quantification of the new bone area/total bone area ratio (n = 6 per group). f, g. Representative IFHC images of the callus region at 28 days and quantification of the relative fluorescence intensities: (f) The white dotted line represents the boundary between the callus and muscles (M: muscle, C: callus); Runx2 (red), ALP (green), and DAPI (blue). Scale bar: 50 μm; (g) Quantification of the relative fluorescence intensities of Runx2 and ALP (n = 6 per group). h, i. Representative IFHC images of the callus region at 28 days and quantification of the relative fluorescence intensities: (h) The white dotted line represents the boundary between the callus and muscles (M: muscle, C: callus); Sp7 (red), ALP (green), and DAPI (blue). Scale bar: 50 μm; (i) Quantification of the relative fluorescence intensities of Sp7 and ALP (n = 6 per group). The data are presented as the means ± standard deviations (SDs). Unpaired Student's t -test was used for two-group comparisons. One-way ANOVA was used for multiple comparisons. Significance levels: ∗ p < 0.05, ∗∗∗∗ p < 0.0001.

    Article Snippet: After blocking with 3% BSA, membranes were incubated with the following primary antibodies: anti-Flag (1:5000, Sigma‒Aldrich, Germany) to detect Bmp2 and D-Bmp2, anti-phospho-Smad1/5/9 (1:1000, Cell Signaling Technology, USA) to assess pathway activation, anti-Runx2 (1:1000, Beyotime, China), and anti-Sp7 (1:1000, MCE, China) to examine osteogenic marker expression.

    Techniques: Micro-CT, Staining, Fluorescence, Muscles