Oligomerization and insertion of antimicrobial peptide TP4 on bacterial membrane and membrane-mimicking surfactant sarkosyl.
Antimicrobial peptides (AMPs) are important components of the host innate defense mechanism against invading microorganisms. Although AMPs are known to act on bacterial membranes and increase membrane permeability, the action mechanism of most AMPs still remains unclear. In this report, we found tha...
Main Authors: | Shih-Han Wang, Chiu-Feng Wang, Ting-Wei Chang, Yu-June Wang, You-Di Liao |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2019-01-01
|
Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0216946 |
Similar Items
-
Sarkosyl differentially solubilizes patient-derived alpha-synuclein fibril strains
by: Hjalte Gram, et al.
Published: (2023-08-01) -
Effectiveness of a Novel Dentifrice Containing Stabilized Chlorine Dioxide, Sarkosyl, and Sodium Fluoride
by: Srinivas Rao Mynenivenkatasatya, et al.
Published: (2020-10-01) -
Surfactant protein C peptides with salt-bridges (“ion-locks”) promote high surfactant activities by mimicking the α-helix and membrane topography of the native protein
by: Frans J. Walther, et al.
Published: (2014-07-01) -
A model membrane approach for interrogating membrane morphological responses induced by membrane-active peptides surfactants
by: Kim, Min Chul
Published: (2017) -
An enhancer peptide for membrane-disrupting antimicrobial peptides
by: Zhang Hong, et al.
Published: (2010-02-01)