A comparative study on interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers

doi:10.1016/0005-2736(91)90082-J

Biochimica et Biophysica Acta (BBA) - Biomembranes

Volume 1070, Issue 2, 9 December 1991, Pages 419-428

https://doi.org/10.1016/0005-2736(91)90082-J Get rights and content

Abstract

Interactions of α-aminoisobutyric acid containing antibiotic peptides, trichopolyn I and hypelcin A with phosphatidylcholine bilayers were investigated to obtain some basic information on their bioactive mechanisms. Trichopolyn I as well as hypelcin A induced the leakage of a fluorescent dye, calcein, entrapped in sonicated egg yolk l-α-phosphatidylcholine vesicles. A quantitative analysis revealed that both the binding affinity and the ‘membrane-perturbing activity’ of trichopolyn I to the vesicles are about one-third of those of hypelcin A. The conformations and the orientations of the peptide and lipid molecules in the membranes were studied using polarized Fourier transform infrared-attenuated total reflection spectroscopy, circular dichroism, and differential scanning calorimetry. In phosphatidylcholine bilayers, both peptides mainly conformed to helical structures irrespective of the membrane physical state (gel or liquid-crystalline). The helix axes, penetrating the hydrophobic region of the bilayers, were oriented neither parallel nor perpendicular to the membrane normal. The disruption in the lipid packing induced by the peptide insertion seems to be responsible for the leakage by these peptides.

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