Journal
LANGMUIR
Volume 27, Issue 10, Pages 5918-5926Publisher
AMER CHEMICAL SOC
DOI: 10.1021/la104814z
Keywords
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Funding
- US Department of Energy, Office of Advanced Scientific Computing [DE-FG02-02ER25535]
- Portuguese Foundation for Science and Technology [SFRH/BPD/20555/2004/0GVL]
- USA National Science Foundation [EEC-0353569]
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We investigate the role of dynamics on adsorption of peptides to gold surfaces using all-atom molecular dynamics simulations in explicit solvent. We choose six homopolypeptides [Ala(10), Ser(10), Thr(10), Arg(10), Lys(10), and Gln(10)], for which experimental surface coverages are not correlated with amino acid level affinities for gold, with the idea that dynamic properties may also play a role. To assess dynamics we determine both conformational movement and flexibility of the peptide within a given conformation. Low conformational movement indicates stability of a given conformation and leads to less adsorption than homopolypeptides with faster conformational movement. Likewise, low flexibility within a given conformation also leads to less adsorption. Neither amino acid affinities nor dynamic considerations alone predict surface coverage; rather both quantities must be considered in peptide adsorption to gold surfaces.
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