Biophysical investigation of the membrane-disrupting mechanism of the antimicrobial and amyloid-like peptide dermaseptin S9.
Dermaseptin S9 (Drs S9) is an atypical cationic antimicrobial peptide with a long hydrophobic core and with a propensity to form amyloid-like fibrils. Here we investigated its membrane interaction using a variety of biophysical techniques. Rather surprisingly, we found that Drs S9 induces efficient...
Main Authors: | Lucie Caillon, J Antoinette Killian, Olivier Lequin, Lucie Khemtémourian |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2013-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3795727?pdf=render |
Similar Items
-
Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage
by: Barend O.W. Elenbaas, et al.
Published: (2023-01-01) -
Antitumor and angiostatic activities of the antimicrobial peptide dermaseptin B2.
by: Hanneke van Zoggel, et al.
Published: (2012-01-01) -
Antitumor Activity and Mechanism of Action of Hormonotoxin, an LHRH Analog Conjugated to Dermaseptin-B2, a Multifunctional Antimicrobial Peptide
by: Mickael Couty, et al.
Published: (2021-10-01) -
Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
by: Daning Shi, et al.
Published: (2016-05-01) -
Dermaseptins, Multifunctional Antimicrobial Peptides: A Review of Their Pharmacology, Effectivity, Mechanism of Action, and Possible Future Directions
by: Emiel Jacob Henri Bartels, et al.
Published: (2019-11-01)