Interaction between Antimicrobial Peptide CM15 and a Model Cell Membrane Affected by CM15 Terminal Amidation and the Membrane Phase State

Antimicrobial peptides (AMPs) have been proposed as an effective class of antimicrobial agents against microorganisms. In this work, the interaction between an antimicrobial peptide, CM15, and a negatively charged phospholipid bilayer, DPPG, was studied via sum frequency generation (SFG) vibrational...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 37(2021), 4 vom: 02. Feb., Seite 1613-1621
1. Verfasser: Ma, Liang (VerfasserIn)
Weitere Verfasser: Luo, Yongsheng, Ma, Yong-Hao, Lu, Xiaolin
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Antimicrobial Cationic Peptides Lipid Bilayers Pore Forming Cytotoxic Proteins
Beschreibung
Zusammenfassung:Antimicrobial peptides (AMPs) have been proposed as an effective class of antimicrobial agents against microorganisms. In this work, the interaction between an antimicrobial peptide, CM15, and a negatively charged phospholipid bilayer, DPPG, was studied via sum frequency generation (SFG) vibrational spectroscopy. Two structurally correlated characteristic variables were introduced to reveal the interaction mechanism/efficiency, i.e. C-terminal amidation and temperature variation (∼20 °C, room temperature, and ∼35 °C, close to human body temperature). Experimental results indicated that owing to the increased positive charge, C-terminal amidation resulted in rapid adsorption onto the bilayer surface and efficient disruption of the outer layer, exhibiting less ordered insertion orientation. The elevated temperature (from ∼20 °C to ∼35 °C) promoted the penetration of both the outer and inner leaflets by the peptides and finally led to the disruption of the whole bilayer owing to the enhanced fluidity of the bilayer. From the perspective of the interaction mechanism, this experimental study provides two practical cues to understand the disruption process of the negatively charged model biomembranes, which can lay the structural foundation for designing and developing high-efficiency antimicrobial peptides
Beschreibung:Date Completed 21.06.2021
Date Revised 21.06.2021
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.0c03498