Modeling the Interaction between Integrin-Binding Peptide (RGD) and Rutile Surface: The Effect of Cation Mediation on Asp Adsorption

• Published in: Langmuir Vol. 28; no. 5; pp. 2799 - 2811
• Main Authors: Wu, Chunya, Skelton, Adam A., Chen, Mingjun, Vlček, Lukas, Cummings, Peter T.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 07.02.2012
• Subjects: Adsorption; Aspartic Acid - chemistry; Cations - chemistry; Chemistry; Exact sciences and technology; General and physical chemistry; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Models, Molecular; Oligopeptides - chemistry; Surface physical chemistry; Surface Properties; Titanium - chemistry; Water - chemistry; Binding; Monovalent cation; Hydration; Peptides; Rutile; Molecular dynamics; Trap; Glycine; Modeling; Surface effect; Geometry; Adsorption; Simulation; Residue; Binding mode; Aspartic acid; Aqueous solution; Divalent cation; Hydroxyl; Hydrogen bond

The binding of a negatively charged residue, aspartic acid (Asp) in tripeptide arginine-glycine-aspartic acid, onto a negatively charged hydroxylated rutile (110) surface in aqueous solution, containing divalent (Mg2+, Ca2+, or Sr2+) or monovalent (Na+, K+, or Rb+) cations, was studied by molecular...