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

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 BK 1–5 ), with anionic vesicles of dimyristoyl phosphatidylglycerol (DMPG). For temperatures above the lipid gel–liquid crystal thermal transition ( T m ≈ 20°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°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°C). That effect could not be assigned to the BK 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 Zn 2+ , and the peptide pentalysine. The data presented here are discussed in the light of the different BK and BK fragments biological activities. © 2000 John Wiley & Sons, Inc. Biopoly 54: 211–221, 2000