How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile

How Insertion of a Single Tryptophan in the N-Terminus of a Cecropin A-Melittin Hybrid Peptide Changes Its Antimicrobial and Biophysical Profile

In the era of antibiotic resistance, there is an urgent need for efficient antibiotic therapies to fight bacterial infections. Cationic antimicrobial peptides (CAMP) are promising lead compounds given their membrane-targeted mechanism of action, and high affinity towards the anionic composition of b...

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Bibliographic Details
Main Authors: Ana Rita Ferreira, Cátia Teixeira, Carla F. Sousa, Lucinda J. Bessa, Paula Gomes, Paula Gameiro
Format: Article
Language:English
Published: MDPI AG 2021-01-01
Series:Membranes
Subjects:
antibiotic resistance
CAMP
cecropin-melittin peptides
tryptophan
cation-π interactions
large unilamellar vesicles
Online Access:https://www.mdpi.com/2077-0375/11/1/48

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