title: Adsorption of homopolypeptides on gold investigated using atomistic molecular dynamics.
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 [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.
authors.affiliation: University of Minho, Department of Physics, Braga, Portugal.
authors.forename: Ana
authors.initials: A
authors.lastname: Vila Verde
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Beltramo
authors.forename: Janna K
authors.initials: JK
authors.lastname: Maranas
mesh_terms: D000327:Adsorption; D006046:Gold / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D055550:Protein Stability; D012996:Solutions; D013499:Surface Properties
chemical_list: D010455:Peptides; D012996:Solutions; D006046:Gold