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Exploring the structural requirements of collagen‐binding peptides
Author(s) -
AbdElgaliel Wael R.,
Tung ChingHsuan
Publication year - 2013
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.22188
Subject(s) - chemistry , peptide , in vitro , residue (chemistry) , biochemistry , amino acid residue , oligopeptide , amino acid , peptide sequence , binding site , sequence (biology) , plasma protein binding , biophysics , stereochemistry , biology , gene
Collagen synthesis and tissue remodeling are involved in many diseases; therefore, collagen‐specific binding agents have been developed to study collagen changes in various tissues. Based on a recently reported collagen binding peptide, which contains unnatural biphenylalanine (Bip) amino acid residue, constructs with various structure variations were synthesized to explore the contributions of unnatural Bip residue, conformational restrain, and amino acid sequence in collagen recognition. Their binding efficiency to collagens was evaluated in vitro using pure collagens. The results indicate that the C‐terminal unnatural Bip residue, rather than the peptide sequence or conformational restrain, dominated the collagen I binding. Subsequent tissue binding study showed that the selected peptide did not offer preferential selectivity over collagen I in tissue, suggesting that a simple in vitro binding assay cannot adequately model the complex biological environment. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 100: 167–173, 2013.