Sequence effects on peptide assembly characteristics observed by using scanning tunneling microscopy

Xiaobo Mao, Yuanyuan Guo, Yin Luo, Lin Niu, Lei Liu, Xiaojing Ma, Huibin Wang, Yanlian Yang, Guanghong Wei, Chen Wang

Research output: Contribution to journalArticle

Abstract

Homogeneous assemblies of the model peptides at interfaces have been achieved and observed with scanning tunneling microscopy. The dependence of the observed brightness in STM images is analyzed, and the correlation with the peptide residues is proposed. We have also investigated the conformational dynamics of the peptide assemblies adsorbed on a graphene sheet by performing all-atom molecular dynamic simulations in water at 300 K. The simulation results of the two peptide assemblies on graphite surfaces show that R 4G4H8 and F4G4H 8 peptide assemblies are mostly in β-sheet structure, and the interaction energy of the four different residues with graphite surfaces follows the order of Phe > His > Arg > Gly, consistent with their brightness contrasts in STM images. The insight on the distribution of residue moieties in the peptide assemblies could provide beneficial venues for studying peptide-based interfacial processes such as site-specific interactions between molecular species with peptides.

Original languageEnglish (US)
Pages (from-to)2181-2187
Number of pages7
JournalJournal of the American Chemical Society
Volume135
Issue number6
DOIs
StatePublished - Feb 13 2013

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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