Molecular packing of lipid membranes and action mechanisms of membrane-active peptides

Pin Chiuan Chiou, Wen Wei Hsu, Yung Chang, Yi Fan Chen

Research output: Contribution to journalArticlepeer-review

Abstract

Biomembranes are involved in diverse cellular activities. How membranes and proteins interact in the activities might hinge on the former's physical characteristics, which in turn are influenced by packing of lipid molecules. Yet, the validity of this understanding and its mechanism are unclear. By varying chain saturation of membranes, we explored correlations between lipid packing and peptide-mediated membrane disruption for the antimicrobial peptide, melittin, and amyloidogenic peptide, β-amyloid (1−42). Remarkably, reducing molecular packing flexibility enhanced the membrane disruption, possibly due to a shift from membrane perforation to micellization. A theoretical analysis suggested the energetic basis of this shift. This mechanistically shows that a peptide's mechanism might be dictated not only by its intrinsic properties but also by physical characteristics of membranes.

Original languageEnglish
Article number112384
JournalColloids and Surfaces B: Biointerfaces
Volume213
DOIs
StatePublished - May 2022

Keywords

  • Melittin
  • Membrane active peptide
  • Membrane pore formation
  • Protein-membrane interactions
  • β-amyloid

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