Photo-initiated rupture of azobenzene micelles to enable the spectroscopic analysis of antimicrobial peptide dynamics

Antimicrobial peptides (AMPs) show promise for the treatment of bacterial infections, but many have undesired hemolytic activities. The AMP MP1 not only has broad spectrum bactericidal activity, but has been shown to have antitumor activity. The interaction between AMPs and cellular membranes gives...

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Bibliographic Details
Published in:RSC advances 2020-06, Vol.1 (36), p.21464-21472
Main Authors: Roberson, Matthew G, Duncan, Julia M, Flieth, Keveen J, Geary, Laina M, Tucker, Matthew J
Format: Article
Language:English
Subjects:
Anticancer properties
Antiinfectives and antibacterials
Azo compounds
Bacterial diseases
Binding
Cell membranes
Chemistry
Deformation
Micelles
NMR
Nuclear magnetic resonance
Peptides
Selectivity
Spectroscopic analysis
Surfactants
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Summary:Antimicrobial peptides (AMPs) show promise for the treatment of bacterial infections, but many have undesired hemolytic activities. The AMP MP1 not only has broad spectrum bactericidal activity, but has been shown to have antitumor activity. The interaction between AMPs and cellular membranes gives rise to a peptide's cell-specificity and activity. However, direct analysis of the biophysical interactions between peptides and membrane is complex, in part due to the nature of membrane environments as well as structural changes in the peptide that occurs upon binding to the membrane. In order to investigate the interplay between cell selectivity, activity, and secondary structural changes involved in antimicrobial peptide activity, we sought to implement photolizable membrane mimics to assess the types of information available from infrared spectroscopic measurements that follow from photoinitiated peptide dynamics. Azo-surfactants (APEG) form micelles containing a photolizable azobenzene core, which upon irradiation can induce membrane deformation resulting in breakdown of micelles. Spectroscopic analysis of membrane deformation may provide insights into the physical behavior associated with unfolding and dissociation of antimicrobial peptides within a membrane environment. Herein, we synthesized and characterized two new azo-surfactants, APEG TMG and APEG NEt 2 MeI . Furthermore, we demonstrate the viability of azosurfactants as membrane mimics by examining both the membrane binding and dissociation induced secondary structural changes of the antimicrobial peptide, MP1. Membrane mediated peptide conformational changes via photo-induced micelle disruption.
ISSN:2046-2069
2046-2069
DOI:10.1039/d0ra01920h