Journal: Nature Communications

Article Title: Superior visible light hydrogen evolution of Janus bilayer junctions via atomic-level charge flow steering

doi: 10.1038/ncomms11480

Figure Lengend Snippet: ( a ) Top-view TEM image, ( b – e ) elemental mapping images, ( f ) XPS spectra, ( h , i ) AFM images, side-view TEM image ( m ) and atomic-resolution HAADF-STEM image ( n ), and ( o – s ) the corresponding EELS elemental maps of BOC-MS. Scale bar, 500 nm, 1 μm, 500 nm, 10 nm and 5 Å, in a , h , i , m , n , respectively. ( g ) S K-edge XANES spectra of BOC-MS, 1L-MS and bulk MS. ( j ) Height profiles along the lines in i . ( k ) Comparison of the average thicknesses of 1L-BOC and 1L-MS in BOC-MS. The error bars in k represent the s.d. of over 100 independent AFM measurements. ( l ) The theoretical thicknesses of MoS 2 and Bi 12 O 17 Cl 2 monolayers.

Article Snippet: At the optimal MoS 2 loading (10 wt%, Supplementary Fig. 8a ) and ascorbic acid concentration (0.3 mol l −1 , ), BOC-MS delivered a PHE rate of 33 mmol h −1 g −1 ( ) and a quantum yield of around 36% at 420 nm , representing the currently achieved state-of-the-art PHE activity among all the MoS 2 -based, monolayer-based and bismuth oxyhalide-based PHE systems ( ).

Techniques:

Journal: Nature Communications

Article Title: Superior visible light hydrogen evolution of Janus bilayer junctions via atomic-level charge flow steering

doi: 10.1038/ncomms11480

Figure Lengend Snippet: ( a ) Charge density contour plots and ( b ) electrostatic potential viewed from the {110} facet of Bi 12 O 17 Cl 2 . XPS spectra of 1L-BOC photo-deposited with different amounts of Pt ( c , d ) and MnO x ( e , f ), demonstrating the interactions between Pt (or MnO x ) and atoms on deposition sites. ( g , k ) The side-view atomic-resolution HAADF-STEM images, and ( h – j , l – n ) the corresponding EELS elemental maps of 1L-BOC photo-deposited with Pt and MnO x . Scale bar, 10 Å in g , k . Comparison of XPS spectra ( q ) and Bi L-edge EXAFS ( r ) of BOC-MS and BOC-MS-Mix, identifying the formation of Bi–S bonds at the interfaces between Bi 12 O 17 Cl 2 and MoS 2 in the Janus bilayer. Comparison of the electrostatic potentials of (Cl 2 )-(Bi 12 O 17 )-(MoS 2 ) with ( s ) and without ( t ) Bi–S bonds. ( u ) Comparison of the build-up dynamics of electrons' excited-state absorption (ESA) signals (pumped at 400 nm and probed at 650 nm) of BOC-MS and BOC-MS-Mix, highlighting the crucial role of Bi–S bonds in steering charge flow from 1L-BOC to 1L-MS in BOC-MS. Schematic illustration of the crystal structure of BOC-MS ( o ) and of the charge flow processes within BOC-MS, including the electron–hole separation within 1L-BOC ( p ) and the interfacial electron transfer from 1L-BOC to 1L-MS along the Bi–S bonds ( v ).

Article Snippet: At the optimal MoS 2 loading (10 wt%, Supplementary Fig. 8a ) and ascorbic acid concentration (0.3 mol l −1 , ), BOC-MS delivered a PHE rate of 33 mmol h −1 g −1 ( ) and a quantum yield of around 36% at 420 nm , representing the currently achieved state-of-the-art PHE activity among all the MoS 2 -based, monolayer-based and bismuth oxyhalide-based PHE systems ( ).

Techniques:

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: Stability (half-life) of peptide hormones in blood specimens.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques: Enzyme-linked Immunosorbent Assay, Tandem Mass Spectroscopy

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: Both G36A and G37 were stable over 4-day incubation in P800 plasma, and their fragments, including G36A-2N and G37-2N, were only detectable after 72 hours. This is representative of 3 subjects.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques: Incubation

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: A. GLP-1 stability in EDTA, P700 and P800 plasma samples. G36A was incubated in EDTA, P700 and P800 plasma samples prepared from the same three healthy individuals. The relative intensity (Rel. Int.) representing the ratios of peak intensity of G36A to AG36 was plotted according to the first-order degradation, and half-lives of the GLP-1 peptides were then determined. The recovery of the peptide is the ratio of the area of the peak for the peptides studied to the area of the control peptide; both peptides are spiked at the same final concentration. B. GLP-1 stability comparison in EDTA and plasma samples with protease inhibitors at room temperature. Four individual plasma samples collected with EDTA, P800, and P700 tubes were incubated with G36A and analyzed by ELISA. The analysis of G36A by ELISA was carried out with pooled plasma samples from 3 subjects with three replicates. The results displayed are representative. The error bars indicated standard deviations of the means from two replicates of four individuals. C. GLP-1 stability in EDTA and P800 plasma samples on ice. The analysis of G36A by ELISA was carried out with pooled plasma samples from 3–4 subjects with three replicates.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques: Incubation, Concentration Assay, Enzyme-linked Immunosorbent Assay

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: Stability (T ½ ) was indicated in the first-order kinetics analysis of GIP in pooled P800, EDTA and serum samples. The relative intensity (Rel. Int,) represented the peak ratio of GIP to the control . Data are representative from 4 subjects with 1 or two replicates.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques:

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: Active G36A was spiked into EDTA, EDTA plus Diprotin A (500 units/mL) and P800 whole blood samples. After incubation at room temperature for indicated time periods, the samples were centrifuged, and plasma portions were taken for ELISA-based peptide analysis. This data is representative of 1 subject with three replicates. A total of 3 subjects were tested and gave similar profiles.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques: Incubation, Enzyme-linked Immunosorbent Assay

Journal: PLoS ONE

Article Title: Degradation and Stabilization of Peptide Hormones in Human Blood Specimens

doi: 10.1371/journal.pone.0134427

Figure Lengend Snippet: Full-length OXM (1–37), fragments OXM-2N and OXM-4N generated by incubation with pure DPP-IV for 24 and 48 h respectively, were spiked into P800 plasma, immediately acidified, and analyzed by EIA. The data are from 3 subjects with 2 replicates.

Article Snippet: Human blood from healthy subjects was directly collected into BD P800 (2.0 mL or 8.5 mL, optimized for the stabilization of GLP-1, GIP, glucagon, and oxyntomodulin), P700 (optimized for GLP-1 stabilization only), K 2 EDTA or serum tubes (BD, Franklin Lakes, NJ) by venipuncture.

Techniques: Generated, Incubation