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The interaction between Au@PEG NPs and hemoglobin, and Au@PEG NPs induce conformational changes and deoxygenation of hemoglobin. (A) Detection of the binding affinity of hemoglobin (1.328 mM) with the Au@PEG NPs (6.95 mM) by isothermal titration calorimetry (ITC). The ITC raw data (top) and the integrated heat data (bottom) in each injection together with the best fit. Binding curve of (B) human albumin (1.6–6.4 mM), (C) hemoglobin (1.6–6.4 mM) with <t>the</t> <t>immobilized</t> Au@PEG NPs microarray detected by <t>SPRi.</t> (D) Circular dichroism spectrum of oxyhemoglobin (1.5 μM), deoxyhemoglobin (1.5 μM), and 1.5 μM hemoglobin treated with Au@PEG NPs (0.05 mM). (E) Raman spectrum of hemoglobin (0.38 mM) in oxygenated condition and hemoglobin treated with Au@PEG NPs (1.00 mM) in oxygenated condition.
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The interaction between Au@PEG NPs and hemoglobin, and Au@PEG NPs induce conformational changes and deoxygenation of hemoglobin. (A) Detection of the binding affinity of hemoglobin (1.328 mM) with the Au@PEG NPs (6.95 mM) by isothermal titration calorimetry (ITC). The ITC raw data (top) and the integrated heat data (bottom) in each injection together with the best fit. Binding curve of (B) human albumin (1.6–6.4 mM), (C) hemoglobin (1.6–6.4 mM) with <t>the</t> <t>immobilized</t> Au@PEG NPs microarray detected by <t>SPRi.</t> (D) Circular dichroism spectrum of oxyhemoglobin (1.5 μM), deoxyhemoglobin (1.5 μM), and 1.5 μM hemoglobin treated with Au@PEG NPs (0.05 mM). (E) Raman spectrum of hemoglobin (0.38 mM) in oxygenated condition and hemoglobin treated with Au@PEG NPs (1.00 mM) in oxygenated condition.
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The interaction between Au@PEG NPs and hemoglobin, and Au@PEG NPs induce conformational changes and deoxygenation of hemoglobin. (A) Detection of the binding affinity of hemoglobin (1.328 mM) with the Au@PEG NPs (6.95 mM) by isothermal titration calorimetry (ITC). The ITC raw data (top) and the integrated heat data (bottom) in each injection together with the best fit. Binding curve of (B) human albumin (1.6–6.4 mM), (C) hemoglobin (1.6–6.4 mM) with the immobilized Au@PEG NPs microarray detected by SPRi. (D) Circular dichroism spectrum of oxyhemoglobin (1.5 μM), deoxyhemoglobin (1.5 μM), and 1.5 μM hemoglobin treated with Au@PEG NPs (0.05 mM). (E) Raman spectrum of hemoglobin (0.38 mM) in oxygenated condition and hemoglobin treated with Au@PEG NPs (1.00 mM) in oxygenated condition.

Journal: International Journal of Pharmaceutics: X

Article Title: PEGylated gold nanoparticles regulate metabolic flux in erythrocytes by inducing hemoglobin deoxygenation

doi: 10.1016/j.ijpx.2026.100495

Figure Lengend Snippet: The interaction between Au@PEG NPs and hemoglobin, and Au@PEG NPs induce conformational changes and deoxygenation of hemoglobin. (A) Detection of the binding affinity of hemoglobin (1.328 mM) with the Au@PEG NPs (6.95 mM) by isothermal titration calorimetry (ITC). The ITC raw data (top) and the integrated heat data (bottom) in each injection together with the best fit. Binding curve of (B) human albumin (1.6–6.4 mM), (C) hemoglobin (1.6–6.4 mM) with the immobilized Au@PEG NPs microarray detected by SPRi. (D) Circular dichroism spectrum of oxyhemoglobin (1.5 μM), deoxyhemoglobin (1.5 μM), and 1.5 μM hemoglobin treated with Au@PEG NPs (0.05 mM). (E) Raman spectrum of hemoglobin (0.38 mM) in oxygenated condition and hemoglobin treated with Au@PEG NPs (1.00 mM) in oxygenated condition.

Article Snippet: To detect the interaction between the immobilized Au@PEG NPs and the flowing proteins, an SPRi instrument (PlexArray HT, Plexera) was used to monitor the whole process in real time.

Techniques: Binding Assay, Isothermal Titration Calorimetry, Injection, Microarray, Circular Dichroism