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  Study of the interaction of a novel semi-synthetic peptide with model lipid membranes

Sessa, L., Concilio, S., Walde, P., Robinson, T., Dittrich, P. S., Porta, A., et al. (2020). Study of the interaction of a novel semi-synthetic peptide with model lipid membranes. Membranes, 10(10): 294. doi:10.3390/membranes10100294.

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 Creators:
Sessa, Lucia, Author
Concilio, Simona, Author
Walde, Peter, Author
Robinson, Tom1, Author              
Dittrich, Petra S., Author
Porta, Amalia, Author
Panunzi, Barbara, Author
Caruso, Ugo, Author
Piotto, Stefano, Author
Affiliations:
1Tom Robinson, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_2288691              

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Free keywords: peptide; MD; GUV; LUV; azo-amino acid
 Abstract: Most linear peptides directly interact with membranes, but the mechanisms of interaction are far from being completely understood. Here, we present an investigation of the membrane interactions of a designed peptide containing a non-natural, synthetic amino acid. We selected a nonapeptide that is reported to interact with phospholipid membranes, ALYLAIRKR, abbreviated as ALY. We designed a modified peptide (azoALY) by substituting the tyrosine residue of ALY with an antimicrobial azobenzene-bearing amino acid. Both of the peptides were examined for their ability to interact with model membranes, assessing the penetration of phospholipid monolayers, and leakage across the bilayer of large unilamellar vesicles (LUVs) and giant unilamellar vesicles (GUVs). The latter was performed in a microfluidic device in order to study the kinetics of leakage of entrapped calcein from the vesicles at the single vesicle level. Both types of vesicles were prepared from a 9:1 (mol/mol) mixture of POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) and POPG (1-palmitoyl-2-oleoyl-sn-glycero-3-phospho(1prime'-rac-glycerol). Calcein leakage from the vesicles was more pronounced at a low concentration in the case of azoALY than for ALY. Increased vesicle membrane disturbance in the presence of azoALY was also evident from an enzymatic assay with LUVs and entrapped horseradish peroxidase. Molecular dynamics simulations of ALY and azoALY in an anionic POPC/POPG model bilayer showed that ALY peptide only interacts with the lipid head groups. In contrast, azoALY penetrates the hydrophobic core of the bilayers causing a stronger membrane perturbation as compared to ALY, in qualitative agreement with the experimental results from the leakage assays.

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Language(s): eng - English
 Dates: 2020-10-192020
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.3390/membranes10100294
BibTex Citekey: membranes10100294
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Title: Membranes
Source Genre: Journal
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Publ. Info: Basel : MDPI
Pages: - Volume / Issue: 10 (10) Sequence Number: 294 Start / End Page: - Identifier: ISSN: 2077-0375