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Magainin 2 and PGLa in bacterial membrane mimics IV: Membrane curvature and partitioning

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SEMERARO E.F. PAJTINKA Peter MARX L. KABELKA Ivo LEBER R. LOHNER K. VÁCHA Robert PABST G.

Rok publikování 2022
Druh Článek v odborném periodiku
Časopis / Zdroj BIOPHYSICAL JOURNAL
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
www https://www.sciencedirect.com/science/article/pii/S0006349522008566#!
Doi http://dx.doi.org/10.1016/j.bpj.2022.10.018
Klíčová slova LIPID-BILAYERSANTIBIOTIC PEPTIDEFORCE-FIELDFLUORESCENCEDYNAMICSSIMULATIONSMECHANISMSYNERGISMFUSIONMODEL
Přiložené soubory
Popis We previously reported that the synergistically enhanced antimicrobial activity of magainin 2 (MG2a) and PGLa is related to membrane adhesion and fusion. Here, we demonstrate that equimolar mixtures of MG2a and L18W-PGLa induce positive monolayer curvature stress and sense, at the same time, positive mean and Gaussian bilayer curvatures already at low amounts of bound peptide. The combination of both abilities—membrane curvature sensing and inducing—is most likely the base for the synergistically enhanced peptide activity. In addition, our coarse-grained simulations suggest that fusion stalks are promoted by decreasing the free-energy barrier for their formation rather than by stabilizing their shape. We also interrogated peptide partitioning as a function of lipid and peptide concentration using tryptophan fluorescence spectroscopy and peptide-induced leakage of dyes from lipid vesicles. In agreement with a previous report, we find increased membrane partitioning of L18W-PGLa in the presence of MG2a. However, this effect does not prevail to lipid concentrations higher than 1 mM, above which all peptides associate with the lipid bilayers. This implies that synergistic effects of MG2a and L18W-PGLa in previously reported experiments with lipid concentrations >1 mM are due to peptide-induced membrane remodeling and not their specific membrane partitioning. Significance
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