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Interaction and structural study of kinin peptide bradykinin and ganglioside monosialylated 1 micelle
Author(s) -
Chatterjee Chiradip,
Mukhopadhyay Chaitali
Publication year - 2005
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20278
Subject(s) - chemistry , micelle , bradykinin , peptide , folding (dsp implementation) , biophysics , aqueous solution , crystallography , stereochemistry , biochemistry , organic chemistry , receptor , electrical engineering , biology , engineering
Partitioning of small proteins and peptides from the aqueous to membrane phase is often coupled with folding. In this work we examine the binding and folding of the kinin peptide, bradykinin (BK), in the presence of the ganglioside monosialylated 1 (GM1) micelle. Using two‐dimensional NMR techniques, we have shown that at low concentration, GM1 micelle is able to induce a turn conformation to BK. A pulsed‐field gradient diffusion NMR study indicated that the peptide partitions into the GM1 micelle with a Δ G part of −3.14 ± 0.03 kcal/mol. A saturation transfer difference (STD) NMR study indicated that the binding is mostly through hydrophobic residues. © 2005 Wiley Periodicals, Inc. Biopolymers 78: 197–205, 2005