Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5654
Title: Study of Bradykinin conformation in the presence of model membrane by Nuclear Magnetic Resonance and molecular modelling
Authors: Bonechi, Claudia 
Ristori, S
Martini, G
Martini, S
Rossi, Claudio 
Keywords: Bradykinin; Monolamellar liposome; NMR; DOPC/DOPE
Issue Date: 2009
Project: None 
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Abstract: 
The conformation of bradykinin (BK), Arg1-Pro2-Pro3-Gly4-Phe5-Ser6-Pro7-Phe8-Arg9, was investigated by Nuclear Magnetic Resonance (NMR) spectroscopy and Monte Carlo simulation in two different media, i.e. in pure aqueous solution and in the presence of phospholipid vesicles. Monolamellar liposomes are a good model for biological membranes and mimic the environment experienced by bradykinin when interacting with G-protein coupled receptors (GPCRs). The NMR spectra showed that lipid bilayers induced a secondary structure in the otherwise inherently flexible peptide. The results of ensemble calculations revealed conformational changes occurring rapidly on the NMR time scale and allowed for the identification of different families of conformations that were averaged to reproduce the NMR observables. These structural results supported the hypothesis of the central role played by the peptide C-terminal domain in biological environments, and provided an explanation for the different biological behaviours observed for bradykinin
Description: 
37061
URI: http://hdl.handle.net/20.500.12779/5654
ISSN: 0005-2736
DOI: 10.1016/j.bbamem.2008.12.019
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