Study of bradykinin conformation in the presence of model membrane by Nuclear Magnetic Resonance and molecular modelling

20Citations
Citations of this article
20Readers
Mendeley users who have this article in their library.

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. © 2008 Elsevier B.V. All rights reserved.

Cite

CITATION STYLE

APA

Bonechi, C., Ristori, S., Martini, G., Martini, S., & Rossi, C. (2009). Study of bradykinin conformation in the presence of model membrane by Nuclear Magnetic Resonance and molecular modelling. Biochimica et Biophysica Acta - Biomembranes, 1788(3), 708–716. https://doi.org/10.1016/j.bbamem.2008.12.019

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free