Position-Dependent Influence of the Three Trp Residues on the Membrane Activity of the Antimicrobial Peptide, Tritrpticin
Antimicrobial peptides (AMPs) constitute promising candidates for the development of new antibiotics. Among the ever-expanding family of AMPs, tritrpticin has strong antimicrobial activity against a broad range of pathogens. This 13-residue peptide has an unusual amino acid sequence that is almost s...
Saved in:
Main Authors: | Mauricio Arias (Author), Leonard T. Nguyen (Author), Andrea M. Kuczynski (Author), Tore Lejon (Author), Hans J. Vogel (Author) |
---|---|
Format: | Book |
Published: |
MDPI AG,
2014-11-01T00:00:00Z.
|
Subjects: | |
Online Access: | Connect to this object online. |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Mercury-Supported Biomimetic Membranes for the Investigation of Antimicrobial Peptides
by: Lucia Becucci, et al.
Published: (2014) -
Structure-Activity Relationship Studies of Substitutions of Cationic Amino Acid Residues on Antimicrobial Peptides
by: Mayu Takada, et al.
Published: (2022) -
Phenylboronic ester-modified polymeric nanoparticles for promoting TRP2 peptide antigen delivery in cancer immunotherapy
by: Qiyan Wang, et al.
Published: (2022) -
TRP Channels in Health and Disease
by: Dietrich, Alexander
Published: (2019) -
Insights into the Adsorption Mechanisms of the Antimicrobial Peptide CIDEM-501 on Membrane Models
by: Daniel Alpízar-Pedraza, et al.
Published: (2024)