Record Details

Antimicrobial activity of an artificially designed peptide against fish pathogens

KRISHI: Publication and Data Inventory Repository

View Archive Info
 
 
Field Value
 
Title Antimicrobial activity of an artificially designed peptide against fish pathogens
Not Available
 
Creator Bhat RAH, Khangembam VC, Thakuria D, Pant V, Tandel RS, Tripathi G, Sarma D
 
Subject Artificial antimicrobial peptide Molecular docking Fish pathogen Antimicrobial activity
 
Description Not Available
Antimicrobial peptides (AMPs) are considered alternatives to classical antibiotics and may become an excellent
candidate for tackling antimicrobial resistance in aquaculture. Designing novel antimicrobial peptides for
curbing antimicrobial resistance in aquaculture is paramount in one health approach. In this study, a short and
compositionally simple peptide, KK16, was designed. KK16 is amphipathic with a net charge of + 6. Molecular
docking results revealed that KK16 has a strong affinity towards two virulence proteins of Aeromonas sobria;
aerolysin and outer membrane protein (omp). The peptide was synthesised using Fmoc-chemistry, and its
antimicrobial efficacy was evaluated in vitro against A.sobria, A. salmonicida, Edwardsiella tarda, A. hydrophila,
Vibrio parahaemolyticus, Pseudomonas aeruginosa, Escherichia coli, Staphylococcus epidermidis and methicillin-
resistant S. aureus. The KK16 AMP showed potent activity against the tested bacterial pathogens as revealed
by the MIC and MBC, ranging from 7.81 to 500 μM, and 15–900 μM, respectively. Moreover, the peptide was
stable at higher temperatures and retained its activity in presence of serum and salt. The peptide displayed less
haemolytic and cytotoxic activity even at higher concentrations. In peptide-DNA binding assay, KK16 showed its
binding potential with bacterial genomic DNA and thus, may interfere with replication. Fluorescent microscopy
revealed the uptake of propidium iodide by peptide treated bacterial cells, indicating its membrane disruption
activity. In in vivo experiment, KK16 peptide completely inhibited the growth of Saprolegnia parasitica fungus at
≥ 30 μM peptide concentrations in embryonated fish eggs. The results indicate that KK16 peptide is stable,
possess potent antibacterial and antifungal activity, less cytotoxic to host cells, and hence may prove to be a
promising anti-infective agent for combating common bacterial and fungal infections
Not Available
 
Date 2023-05-12T04:05:02Z
2023-05-12T04:05:02Z
2022-04-08
 
Type Journal
 
Identifier Not Available
Not Available
http://krishi.icar.gov.in/jspui/handle/123456789/77150
 
Language English
 
Relation Not Available;
 
Publisher Elsevier