DFT computational study of the RGD peptide interaction with the rutile TiO2 (110) surface

被引：29

作者：

Muir, J. M. R. ^{[1
]}

Costa, D. ^{[2
]}

Idriss, H. ^{[1
]}

机构：

[1] Univ Aberdeen, Dept Chem, Aberdeen, Scotland

[2] ENSCP, Inst Rech Chim Paris, UMR8247, Chim Paristech CNRS, F-75005 Paris, France

来源：

SURFACE SCIENCE | 2014年 / 624卷

关键词：

Rutile TiO2 (110); Bioinorganic surfaces; Arginine-glycine-aspartic acid (RGD); Ab initio molecular dynamics; Adsorption energy; Carboxylate; AB-INITIO; ENERGY CALCULATIONS; ADSORPTION; TIO2(110); GLYCINE; DYNAMICS; ACID; FIBRONECTIN; PROLINE; CELL;

D O I：

10.1016/j.susc.2014.01.005

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Planewave OFT calculations including ab initio molecular dynamics (AIMD) were used to model the adsorption of a biologically relevant peptide sequence, arginine-glycine-aspartic acid (RGD), upon a rutile TiO2 (110) surface. It was found that binding is solely through the aspartic acid end of the RGD. The carboxy groups bind through dissociative bridging and molecular forms, similar to formic acid. The energy of adsorption is much smaller (0.5-0.77 eV) than seen for formic acid and the molecular adsorption is the strongest adsorption mode. Neutral adsorption is favoured over zwitterionic adsorption and adsorption through the carboxy group of the aspartic acid side chain rather than the terminal carboxy group is favoured due to a configuration allowing an additional surface-carbonyl bond. The RGD backbone is not significantly disrupted upon adsorption. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：8 / 14

页数：7

共 44 条

[21] Exploration of the Conformational and Reactive Dynamics of Glycine and Diglycine on TiO2: Computational Investigations in the Gas Phase and in Solution [J].