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Membrane Binding Properties of Plant Defensins Publisher Pubmed



Shahmiri M1, 3 ; Bleackley MR2 ; Dawson CS2 ; Van Der Weerden NL2 ; Anderson MA2 ; Mechler A1
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Authors Affiliations
  1. 1. Department of Chemistry and Physics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, 3086, VIC, Australia
  2. 2. Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, 3086, VIC, Australia
  3. 3. Department of Medical Nanotechnology, School of Advanced Technologies in Medicine (SATiM), Tehran University of Medical Sciences, Tehran, Iran

Source: Phytochemistry Published:2023


Abstract

The membrane interaction characteristics of five antifungal plant defensin peptides: NaD1, and the related HXP4 and L5, as well as NaD2 and the related ZmD32 were studied. These peptides were chosen to cover a broad range of cationic charges with little structural variations, allowing for assessment of the role of charge in their membrane interactions. Membrane permeabilizing activity against C. albicans was confirmed and quantified for benchmarking purposes. Viscoelastic characteristics of the membrane interactions were studied in typical neutral and charged model membranes using quartz crystal microbalance with dissipation (QCM-D. Frequency-dissipation fingerprinting analysis of the QCM-D results revealed that all of the peptides were able to bind to all studied model membranes albeit with slightly different viscoelastic character for each membrane type. However, characteristic disruption patterns were not observed suggesting that the membrane disrupting activity of these defensins is mostly specific to fungal membranes, and that increasing the peptide charge does not enhance their action. The results also show that the presence of specific sterols has a profound effect on the ability of the peptides to disrupt the membrane. © 2023 Elsevier Ltd
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