Journal: ACS Omega

Article Title: Design and Evaluation of Short Self-Assembling Depsipeptides as Bioactive and Biodegradable Hydrogels

doi: 10.1021/acsomega.7b01641

Figure Lengend Snippet: Half inhibition (i.e., IC 50 ) of the fluorescence of FITC-GRGDSP occurs at a ∼40-fold lower concentration for RGD than R-Glc-D, indicating greater affinity of RGD for integrin than R-Glc-D (A). Comparison of FP inhibition by R-Glc-D and RGE peptides (negative control). The average IC 50 value for R-Glc-D is 1115 ± 211 μM (mean ± standard deviation). RGE was tested once as a negative control, and the calculated IC 50 value was 2840 μM (B).

Article Snippet: Human recombinant integrin α 5 β 1 (R&D Systems) was diluted to 900 nM in the same Tris buffer.

Techniques: Inhibition, Fluorescence, Concentration Assay, Comparison, Negative Control, Standard Deviation

Journal: ChemistryOpen

Article Title: Insights into the Binding of Cyclic RGD Peptidomimetics to α 5 β 1 Integrin by using Live‐Cell NMR And Computational Studies

doi: 10.1002/open.201600112

Figure Lengend Snippet: Docking best poses of a) compound 7 (green) and b) compound 6 (green) in the crystal structure of the extracellular domain of α 5 β 1 integrin (α 5 subunit pink, β 1 subunit cyan, model from 3VI4.pdb). Only selected integrin residues involved in interactions with the ligand are shown. Non polar hydrogens are hidden for clarity, whereas intermolecular hydrogen bonds are shown as dashed lines.

Article Snippet: Purified recombinant human integrin α 5 β 1 (R&D Systems, Inc., Minneapolis, MN, USA) was diluted to 0.5 μg mL −1 in coating buffer containing 20 m m Tris‐HCl (pH 7.4), 150 m m NaCl, 1 m m MnCl 2 , 2 m m CaCl 2 , and 1 m m MgCl 2 .

Techniques:

Journal: ChemistryOpen

Article Title: Insights into the Binding of Cyclic RGD Peptidomimetics to α 5 β 1 Integrin by using Live‐Cell NMR And Computational Studies

doi: 10.1002/open.201600112

Figure Lengend Snippet: Docking binding modes: a) A and b) B of compound 3 (green) in the crystal structure of the extracellular domain of α 5 β 1 integrin (α 5 subunit pink, β 1 subunit cyan, model from 3VI4.pdb). Only selected integrin residues involved in interactions with the ligand are shown. Non polar hydrogens are hidden for clarity, whereas intermolecular hydrogen bonds are shown as dashed lines.

Article Snippet: Purified recombinant human integrin α 5 β 1 (R&D Systems, Inc., Minneapolis, MN, USA) was diluted to 0.5 μg mL −1 in coating buffer containing 20 m m Tris‐HCl (pH 7.4), 150 m m NaCl, 1 m m MnCl 2 , 2 m m CaCl 2 , and 1 m m MgCl 2 .

Techniques: Binding Assay

Journal: ChemistryOpen

Article Title: Insights into the Binding of Cyclic RGD Peptidomimetics to α 5 β 1 Integrin by using Live‐Cell NMR And Computational Studies

doi: 10.1002/open.201600112

Figure Lengend Snippet: Inhibition of biotinylated fibronectin binding to α 5 β 1 integrin compared with inhibition of biotinylated vitronectin binding to α v β 3 .

Article Snippet: Purified recombinant human integrin α 5 β 1 (R&D Systems, Inc., Minneapolis, MN, USA) was diluted to 0.5 μg mL −1 in coating buffer containing 20 m m Tris‐HCl (pH 7.4), 150 m m NaCl, 1 m m MnCl 2 , 2 m m CaCl 2 , and 1 m m MgCl 2 .

Techniques: Inhibition, Binding Assay