Cholesterol, lanosterol, and ergosterol attenuate the membrane association of LL-37(W27F) and temporin L |
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Authors: | Rohit Sood |
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Affiliation: | Helsinki Biophysics and Biomembrane Group, Medical Biochemistry, Institute of Biomedicine, P.O. Box 63 (Haartmaninkatu 8), FIN-00014, University of Helsinki, Finland |
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Abstract: | Sterols impart significant changes to the biophysical properties of lipid bilayers. In this regard the impact of cholesterol on membrane organization and dynamics is particularly well documented and serves for comparison with other sterols. However, the factors underlying the molecular evolution of cholesterol remain enigmatic. To this end, cholesterol attenuates membrane perturbation by the so-called antimicrobial peptides (AMPs), produced ubiquitously by eukaryotic cells to combat bacterial infections by compromising the permeability barrier function of the microbial target membranes. In the present study, we addressed the effects of cholesterol, ergosterol, and lanosterol on the membrane association of two structurally and functionally diverse AMPs viz. LL-37(F27W) and temporin L (TemL) using fluorescence spectroscopy. Interestingly, sterol concentration dependent effects on the membrane association of these peptides were observed. At XSterol = 0.5 cholesterol was most effective in reducing the membrane intercalation of both LL-37(F27W) and TemL, the corresponding efficiencies of the three sterols decreasing as cholesterol > lanosterol ≥ ergosterol, and cholesterol > lanosterol > ergosterol. It is conceivable that part of the selection pressure for the chemical evolution of cholesterol may have derived from the ability to protect the AMP-secreting host cell from the membrane damaging action of the antimicrobial peptides. |
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Keywords: | AMPs, antimicrobial peptides kq, bimolecular quenching constant Chol, cholesterol Ergo, ergosterol EDTA, ethylenediaminetetraacetic acid Lano, lanosterol LL-37 (F27W), LL-37 with Phe27 replaced by Trp LL-37, native LL-37 L/P, lipid/peptide ratio LUV, large unilamellar vesicles lo, liquid ordered phase ld, liquid disordered phase M1, order parameter from NMR PC, phosphatidylcholine PG, phosphatidylglycerol P/L, peptide/lipid ratio Q, quencher Spm, sphingomyelin SOPC, 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine So, solid ordered phase KSV, Stern-Volmer quenching constant λmax, fluorescence emission maximum TemL, temporin L |
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