Další formáty:
BibTeX
LaTeX
RIS
@proceedings{58250,
author = {Khodam Hazrati, Mehrnoosh and Vácha, Robert},
booktitle = {EBSA Congress 2023},
keywords = {antimicrobial peptides; buforin 2; intracelular interactions; buforin 2 membrane translocation},
language = {eng},
title = {Membrane adsorption enhances translocation of antimicrobial peptide buforin 2},
url = {https://mkon.nu/ebsa/scientific_program},
year = {2023}
}
TY - CONF
ID - 58250
AU - Khodam Hazrati, Mehrnoosh - Vácha, Robert
PY - 2023
TI - Membrane adsorption enhances translocation of antimicrobial peptide buforin 2
KW - antimicrobial peptides
KW - buforin 2
KW - intracelular interactions
KW - buforin 2 membrane translocation
UR - https://mkon.nu/ebsa/scientific_program
N2 - Antibiotic resistance has been identified as one of the top three threats to human public health. Promising alternatives to antibiotics are antimicrobial peptides (AMPs) that can selectively kill bacterial cells. Buforin 2 (BF2) is an AMP that kills bacteria via intracellular interactions rather than membrane lysis. BF2 membrane translocation is known to be independent of any cellular receptor because BF2 can readily enter bacterial cells and vesicles that contain only lipids in their membrane. However, the free energy barrier for BF2 translocation across a symmetric membrane suggests a non-spontaneous process, demonstrating our poor understanding of the molecular details of how BF2 crosses biological membranes. Here, we show that inducing membrane asymmetry by BF2 adsorption on one leaflet significantly enhances BF2 translocation across bilayers, indicating that membrane asymmetry may act as a driving force for membrane transport. Our results shed light on the crowding effect of AMP on antibacterial activity and are expected to be helpful in the design of new AMPs.
ER -
KHODAM HAZRATI, Mehrnoosh a Robert VÁCHA. Membrane adsorption enhances translocation of antimicrobial peptide buforin 2. In \textit{EBSA Congress 2023}. 2023.
|
