Investigations on the membrane interaction of C-terminally amidated esculentin-2 HYba1 and 2 peptides against bacteria

The membrane interaction and damage caused by C-terminally amidated esculentin-2 peptides identified from the frog skin is illustrated in the present study using Staphylococcus aureus and Vibrio cholerae. Double staining with fluorescent probes SYTOX and DAPI proved the concentration-dependent bacte...

Full description

Saved in:
Bibliographic Details
Published in:Animal biotechnology 2021-04, Vol.32 (2), p.137-146
Main Authors: Vineeth Kumar, T., Asha, R., George, Sanil
Format: Article
Language:English
Subjects:
Antagonism
Antiinfectives and antibacterials
Antimicrobial activity
Bacteria
Binding sites
Calcium
Calcium ions
Cations
Cell fusion
Combinatorial analysis
Damage
Depolarization
Elongation
Esculentin
Fluorescent indicators
Hydrophylax
Magnesium
membrane action
Membranes
Minimum inhibitory concentration
Peptides
Pores
self-promoted uptake
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The membrane interaction and damage caused by C-terminally amidated esculentin-2 peptides identified from the frog skin is illustrated in the present study using Staphylococcus aureus and Vibrio cholerae. Double staining with fluorescent probes SYTOX and DAPI proved the concentration-dependent bacterial membrane damage induced by the peptides. It was found that the sub-MIC of both peptides induced transient pores on the bacterial membrane. These peptides also caused depolarisation on the bacterial membrane during their interaction. The physical changes on bacterial cells like blebbing, elongation, fusion, and so forth upon peptide treatment were visualized through SEM images. The antimicrobial activity of the peptides against S. aureus and V. cholerae was not altered at physiological concentrations of divalent and monovalent cations, which is advantageous in a therapeutic context. The increase of MIC against V. cholerae at higher concentrations of Mg 2+ and Ca 2+ (>5 µM) is due to the concentration-dependent antagonism exhibited by these ions for the cation binding sites on the bacterial membrane, which facilitates the process of 'self-promoted uptake.' The study emphasizes to utilize the ability of these peptides to produce transient pores at sub-MICs in combinatorial therapy.
ISSN:1049-5398
1532-2378
DOI:10.1080/10495398.2019.1668402