A Recombinant Snake Cathelicidin Derivative Peptide: Antibiofilm Properties and Expression in Escherichia coli.

ABSTRACT: The emergence of antimicrobial resistance among pathogenic microorganisms has been led to an urgent need for antibiotic alternatives. Antimicrobial peptides (AMPs) have been introduced as promising therapeutic agents because of their remarkable potentials. A new modified cathelicidin-BF peptide (Cath-A) with 34 amino acid sequences, represents the potential antimicrobial effects against methicillin-resistant Staphylococcus aureus (MRSA) with slight hemolytic and cytotoxic activities on eukaryotic cells. In this study, the effects of Cath-A on Acinetobacter baumannii, and Pseudomonas aeruginosa isolated from medical instruments were studied. Cath-A inhibited the growth of bacterial cells in the range of 8⁻16 μg/mL and 16-≥256 μg/mL for A. baumannii and P. aeruginosa, respectively. The pepti

SUBMITTER: Tajbakhsh M 

PROVIDER: S-EPMC6315654 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature