Studies on a new antimicrobial peptide from Vibrio proteolyticus MT110

The marine environment is known for its vast diversity of the microbial population; however, less explored for bioactive compounds. In this study, an AMP produced by a new marine isolate, Vibrio proteolyticus MT110, showed broad-spectrum antimicrobial activity against Gram-positive and Gram-negative...

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Bibliographic Details
Published in:Preparative biochemistry & biotechnology 2024-02, Vol.54 (2), p.193-206
Main Authors: Verma, Himanshu, Mihooliya, Kanti N., Nandal, Jitender, Sahoo, Debendra K.
Format: Article
Language:English
Subjects:
Acetic acid
amino acid analysis
Amino acids
Anti-Bacterial Agents - pharmacology
Antibacterial activity
Antimicrobial activity
Antimicrobial agents
Antimicrobial peptide
Antimicrobial Peptides
Bacteria
Bioactive compounds
Biological activity
Drug development
Ethyl acetate
Gram-Negative Bacteria
Gram-Positive Bacteria
Homogeneity
Isoleucine
Liquid chromatography
Marine ecology
Marine environment
MIC
Microbial Sensitivity Tests
Microorganisms
Molecular weight
Peptides
Physicochemical properties
Production methods
response surface methodology
Stability
Statistical methods
Tyrosine
Vibrio
Vibrio proteolyticus
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Summary:The marine environment is known for its vast diversity of the microbial population; however, less explored for bioactive compounds. In this study, an AMP produced by a new marine isolate, Vibrio proteolyticus MT110, showed broad-spectrum antimicrobial activity against Gram-positive and Gram-negative bacteria. The AMP was purified to homogeneity using ethyl acetate extraction followed by RP-HPLC, and LC-MS analysis showed its molecular weight as 980 Da. The MIC of AMP (peptide-MT110) was obtained in the 7.81-31.25 µg/mL range against different indicator strains. Peptide-MT110 showed stability of its antimicrobial activity at 15-121 °C and pH 4-10 and in the presence of various hydrolytic enzymes. The peaks at 1536 cm −1 and 1712 cm −1 wavenumbers in FTIR spectra confirmed the peptidic nature of AMP, and its amino acid analysis confirmed the presence of tyrosine and isoleucine. The antibacterial activity of peptide-MT110 is confirmed by PI assay and TEM. The optimization of peptide-MT110 production using statistical methods resulted in a 2.64-fold higher production. The physicochemical properties and stability in wide pH and temperature ranges showed the potential of peptide-MT110 for its development as a drug candidate. This is believed to be the first report on an AMP from Vibrio proteolyticus.
ISSN:1082-6068
1532-2297
DOI:10.1080/10826068.2023.2209892