End-tagging of ultra-short antimicrobial peptides by W/F stretches to facilitate bacterial killing.
BACKGROUND: Due to increasing resistance development among bacteria, antimicrobial peptides (AMPs), are receiving increased attention. Ideally, AMP should display high bactericidal potency, but low toxicity against (human) eukaryotic cells. Additionally, short and proteolytically stable AMPs are des...
Main Authors: | Mukesh Pasupuleti, Artur Schmidtchen, Anna Chalupka, Lovisa Ringstad, Martin Malmsten |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2009-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC2667214?pdf=render |
Similar Items
-
Highly selective end-tagged antimicrobial peptides derived from PRELP.
by: Martin Malmsten, et al.
Published: (2011-01-01) -
Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutase
by: Schmidtchen Artur, et al.
Published: (2009-07-01) -
Proteolysis of human thrombin generates novel host defense peptides.
by: Praveen Papareddy, et al.
Published: (2010-04-01) -
Interaction Between Antimicrobial Peptides and Phospholipid Membranes : Effects of Peptide Length and Composition
by: Ringstad, Lovisa
Published: (2009) -
Tryptophan end-tagging for promoted lipopolysaccharide interactions and anti-inflammatory effects
by: Shalini Singh, et al.
Published: (2017-03-01)