The influence of amino acid sequence and functionality on the binding process of peptides onto gold surfaces.

Published

Journal Article

We present a molecular dynamics study of the binding process of peptide A3 (AYSSGAPPMPPF) and other similar peptides onto gold surfaces, and identify the functions of many amino acids. Our results provide a clear picture of the separate regimes present in the binding process: diffusion, anchoring, crawling and binding. Moreover, we explored the roles of individual residues. We found that tyrosine, methionine, and phenylalanine are strong binding residues; serine serves as an effective anchoring residue; proline acts as a dynamic anchoring point, while glycine and alanine give flexibility to the peptide backbone. We then show that our findings apply to unrelated phage-derived sequences that have been reported recently to facilitate AuNP synthesis. This new knowledge may aid in the design of new peptides for the synthesis of gold nanostructures with novel morphologies.

Full Text

Duke Authors

Cited Authors

  • Yu, J; Becker, ML; Carri, GA

Published Date

  • January 2012

Published In

Volume / Issue

  • 28 / 2

Start / End Page

  • 1408 - 1417

PubMed ID

  • 22148960

Pubmed Central ID

  • 22148960

Electronic International Standard Serial Number (EISSN)

  • 1520-5827

International Standard Serial Number (ISSN)

  • 0743-7463

Digital Object Identifier (DOI)

  • 10.1021/la204109r

Language

  • eng