title: Single-molecule imaging of gold-binding peptide adsorbed on Au(111).
abstract: Inorganic-binding peptides, which exhibit specific binding affinity to an inorganic material, are versatile building blocks in the construction of novel bio-conjugated materials. However, very little knowledge regarding their adsorbed structures on the target material is currently available. In this article, we report on the single-molecule analysis of such polypeptides by scanning tunneling microscopy (STM). The adsorbed structure of a gold-binding peptide (GBP) on Au(111) was observed at the single-molecule level. FTIR spectroscopy revealed the helical structure of the GBP, and ab initio calculations confirmed the correlation between the observed STM image and a sample helical structure. It has been demonstrated that the conformational structure of the polypeptide is highly pre-organized, allowing favorable binding onto the gold surface. Gaining such an insight into the relation between the structure and the binding function of the peptide leads to a fundamental understanding of inorganic-binding peptide, and, consequently, to a rational design of these peptides.
authors.affiliation: Department of Physics and Electronics, Graduate School of Engineering, Osaka Prefecture University, Sakai, Osaka, Japan.
authors.forename: Satoshi
authors.initials: S
authors.lastname: Kanata
authors.forename: Tomoaki
authors.initials: T
authors.lastname: Nishino
authors.forename: Rie
authors.initials: R
authors.lastname: Makiura
authors.forename: Sho
authors.initials: S
authors.lastname: Saiki
authors.forename: Nobuhiko
authors.initials: N
authors.lastname: Hayashi
mesh_terms: D000327:Adsorption; D000595:Amino Acid Sequence; D006046:Gold / Q000737:chemistry*; D016252:Microscopy, Scanning Tunneling / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013499:Surface Properties
chemical_list: D010455:Peptides; D006046:Gold