Abstract
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 [Ala10, Ser10, Thr10, Arg10, Lys10, and Gln10], 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.
Original language | English (US) |
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Pages (from-to) | 5918-5926 |
Number of pages | 9 |
Journal | Langmuir |
Volume | 27 |
Issue number | 10 |
DOIs | |
State | Published - Jun 1 2011 |
All Science Journal Classification (ASJC) codes
- General Materials Science
- Condensed Matter Physics
- Surfaces and Interfaces
- Spectroscopy
- Electrochemistry