Permeabilization of reconstituted Lipid Bilayers containing mycobacterial TDM through the AMP LL32: Insights into Membrane-Peptide Interactions

This study focuses on the permeabilization behavior of lipid bilayer membranes composed of natural and synthetically produced phosphatidylcholines, in the presence of mycobacterial glycolipid trehalose-6,6’-dimycolate (TDM). The experiments were conducted in the presence of the alpha-helical antimicrobial peptide (AMP) LL32, known for its ability to interact with and disrupt lipid bilayers. Reconstituted lipid bilayers were used to model the biological membrane and to investigate the influence of TDM on the interactions between LL32 and the lipid bilayer. By evaluating membrane integrity, the results provide insights into the effects of TDM on membrane stability and peptide-lipid interactions. This research helps to understand the modulation of membrane integrity by lipids and their role in peptide-mediated permeabilization, with implications for antimicrobial mechanisms and potential future therapeutic applications.

Institutions

Publication Details

Journal
Infinite Science GmbH
Published
2025-01-22
DOI
https://doi.org/10.18416/scp.2025.1960
Primary Topic
Antimicrobial Peptides and Activities
Type
article
Field-Weighted Citation Impact
0.00
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Permeabilization of reconstituted Lipid Bilayers containing mycobacterial TDM through the AMP LL32: Insights into Membrane-Peptide Interactions

Infinite Science GmbH
Antimicrobial Peptides and Activities
article

Permeabilization of reconstituted Lipid Bilayers containing mycobacterial TDM through the AMP LL32: Insights into Membrane-Peptide Interactions

article en

Abstract

This study focuses on the permeabilization behavior of lipid bilayer membranes composed of natural and synthetically produced phosphatidylcholines, in the presence of mycobacterial glycolipid trehalose-6,6’-dimycolate (TDM). The experiments were conducted in the presence of the alpha-helical antimicrobial peptide (AMP) LL32, known for its ability to interact with and disrupt lipid bilayers. Reconstituted lipid bilayers were used to model the biological membrane and to investigate the influence of TDM on the interactions between LL32 and the lipid bilayer. By evaluating membrane integrity, the results provide insights into the effects of TDM on membrane stability and peptide-lipid interactions. This research helps to understand the modulation of membrane integrity by lipids and their role in peptide-mediated permeabilization, with implications for antimicrobial mechanisms and potential future therapeutic applications.

Infinite Science GmbH
Research Center Borstel - Leibniz Lung Center (DE), University of Lübeck (DE)
Openalex Percentile: Top 37%
Antimicrobial Peptides and Activities
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Permeabilization of reconstituted Lipid Bilayers containing mycobacterial TDM through the AMP LL32: Insights into Membrane-Peptide Interactions · Infinite Science GmbH (2025) | TGRS Research Map | TGRS