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Molecular Dynamics Simulation of the Binding Interaction between Hormone Glucagon Protein and Self‐Assembled Monolayer Molecules
Author(s) -
Wang YengTseng,
Cheng ChengLung,
Shih YuChing,
Kan HengChuan,
Chen ChangHung,
Hu JeuJiun,
Su ZhiYuan
Publication year - 2007
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.200790203
Subject(s) - chemistry , monolayer , molecular dynamics , peptide , self assembled monolayer , molecule , stereochemistry , computational chemistry , biochemistry , organic chemistry
Restrained molecular dynamics simulations were performed to study the binding affinity of the peptide with alkanethiols of different tail‐groups, S(CH 2 ) 7 CH 3 , S(CH 2 ) 7 OH and S(CH 2 ) 7 COOH, 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>CH 3 ‐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.