期刊
COLLOIDS AND SURFACES B-BIOINTERFACES
卷 67, 期 2, 页码 157-165出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.colsurfb.2008.07.011
关键词
Antimicrobial peptide; Surface structure
资金
- U.S. Army NSRDEC [AH52]
The surface structure of an antimicrobial peptide, cecropin P1, immobilized to a gold surface via a terminal cysteine residue was investigated. Using reflection-absorption infrared spectroscopy, surface plasmon resonance, and X-ray photoelectron spectroscopy, the effects of pH,solution conformation, and concentration on the immobilized peptide conformation, average orientation, and surface density were determined. Under all conditions investigated, the immobilized peptides were a-helical in a predominately flat, random orientation. The addition of the reducing agent Tris(2-carboxyethyl) phosphine hydrochloride to the buffer resulted in a twofold increase in immobilized peptide surface density. Published by Elsevier B.V.
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