Molecular Dynamics Simulation of the Binding Interaction between Hormone Glucagon Protein and Self-Assembled Monolayer Molecules

Restrained molecular dynamics simulations were performed to study the binding affinity of the peptide with alkanethiols of different tail‐groups, S(CH2)7CH3, S(CH2)7OH and S(CH2)7COOH, which self‐assembled on Au(111) surface in the presence of water molecules. The curves of binding affinity were cal...

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Bibliographic Details
Published in:Chinese journal of chemistry 2007-08, Vol.25 (8), p.1090-1093
Main Authors: Wang, Yeng-Tseng, Cheng, Cheng-Lung, Shih, Yu-Ching, Kan, Heng-Chuan, Chen, Chang-Hung, Hu, Jeu-Jiun, Su, Zhi-Yuan
Format: Article
Language:English
Subjects:
alkanethiol
binding affinity
molecular dynamics simulations
self-assembled monolayer
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Summary:Restrained molecular dynamics simulations were performed to study the binding affinity of the peptide with alkanethiols of different tail‐groups, S(CH2)7CH3, S(CH2)7OH and S(CH2)7COOH, which self‐assembled on Au(111) surface in the presence of water molecules. The curves of binding affinity were calculated by fixing the center of mass of the peptide at various distances from the assembling surface. Simulation results show that the binding affinity is in the order as COOH‐SAMs>OH‐SAMs>CH3‐SAMs, while 100% COOH‐SAMs>5% COOH‐SAMs in concentration. The effects on binding affinity by different tail‐groups were also studied. Results show that the binding affinity between COOH‐SAMs and the peptide is bigger than those of the others and increasing the acidity of COOH‐SAMs will result in stronger attractive power.
ISSN:1001-604X
1614-7065
DOI:10.1002/cjoc.200790203