How bradykinin alters the lipid membrane structure: A spin label comparative study with bradykinin fragments and other cations

How bradykinin alters the lipid membrane structure: A spin label comparative study with bradykinin fragments and other cations

Author Turchiello, R. F. Google Scholar
Juliano, L. Google Scholar
Ito, A. S. Google Scholar
Lamy-Freund, M. T. Google Scholar
Institution Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Abstract Electron spin resonance spectroscopy of several different spin labels was used to comparatively study the interaction of the cationic peptide hormone bradykinin (BK; Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg), and some BK fragments (des-Arg(9)-BK, des-Arg(1)-BK, and Arg-Pro-Pro-Gly-Phe or BK1-5), with anionic vesicles of dimyristoyl phosphatidylglycerol (DMPG). for temperatures above the lipid gel-liquid crystal thermal transition (T-m approximate to 20 degrees C), membrane-incorporated spin labels indicated that all peptides (total concentration of 10 mol % relative to lipid) interact with the bilayer, turning the membrane less fluid both at its surface and center, suggesting a partial penetration of the peptides into the membrane core. However, in the lipid gel phase (t < T-m), BK was found to display a much stronger interaction with the membrane decreasing the bilayer fluidity. At temperatures around 15 degrees C the BK-DMPG system was found to present a hysteresis, evinced by the different electron spin resonance spectra yielded upon cooling and heating the sample. System reversibility was found at all other temperatures (0-45 degrees C). That effect could not be assigned to the BET higher concentration at the membrane surface due to its higher net charge (2(+)) compared to the fragments (1(+)), because ten times more des-Arg(9)-BK (100 mol %) yielded opposite result. Further, that was found to be a result rather different from those elicited by the other cations tested: the monovalent Na+, the divalent Zn2+, and the peptide pentalysine. the data presented here are discussed in the light of the different BK and BK fragments biological activities. (C) 2000 John Wiley & Sons, Inc.
Keywords bradykinin
dimyristoyl phosphatidylglycerol vesicle
spin label
peptide-lipid interaction
bradykinin fragments
Language English
Date 2000-09-01
Published in Biopolymers. New York: John Wiley & Sons Inc, v. 54, n. 3, p. 211-221, 2000.
ISSN 0006-3525 (Sherpa/Romeo, impact factor)
Publisher Wiley-Blackwell
Extent 211-221
Access rights Closed access
Type Article
Web of Science ID WOS:000088235800007

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