Characterization of Novel Antimicrobial Peptides from the Epidermis of Clarias batrachus Catfish

In this study, an antimicrobial protein (AMP) from the epidermis of catfish ( Clarias batrachus ) was purified and characterized for its molecular and antimicrobial properties. The crude epidermal extract was subjected to precipitation of proteins using 70% ammonium sulphate saturation followed by d...

Full description

Saved in:
Bibliographic Details
Published in:International journal of peptide research and therapeutics 2024-02, Vol.30 (2), p.11, Article 11
Main Authors: Giridharan, Bupesh, Chinnaiah, Amutha, Saravanan, Konda Mani, Parthasarathy, Sudharsan, Meenakshi Sundaram, Kishore Kumar, Tharumasivam, Siva Vijayakumar, Pankaj, Pranay Punj, Govindaraju, Archunan, Haripriya, Dayalan, Sahoo, Uttam Kumar
Format: Article
Language:English
Subjects:
Ammonium sulfate
Animal Anatomy
Antimicrobial activity
Antimicrobial agents
Antimicrobial peptides
Bacteria
Biochemistry
Biomedical and Life Sciences
Clarias batrachus
Clinical isolates
Dialysis
Epidermis
Histology
Life Sciences
Mass spectroscopy
Molecular Medicine
Molecular weight
Morphology
Multidrug resistance
Peptides
Pharmaceutical Sciences/Technology
Pharmacology/Toxicology
Polymer Sciences
Protein purification
Proteins
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:In this study, an antimicrobial protein (AMP) from the epidermis of catfish ( Clarias batrachus ) was purified and characterized for its molecular and antimicrobial properties. The crude epidermal extract was subjected to precipitation of proteins using 70% ammonium sulphate saturation followed by dialysis and protein separation by reverse phase ultra fast liquid chromotography (UFLC) using the C 18 column. The active peptides obtained from fractions 1, 2, and 3 were screened for antimicrobial activity against different bacterial pathogens with a minimum 5 mg/ml inhibitory concentration. An active fraction with a retention time (RT) of 27.069 from the UFLC chromatogram exhibited significant antimicrobial activity against broad-spectrum bacterial and fungal organisms, including multidrug-resistant clinical isolates. The RT 27.069, identified as cationic AMP of fraction-3, has a molecular weight of 25 kDa as determined by MALDI-TOF mass spectrometry. Further studies by Mascot search and BLAST analysis using the partial sequence of AMP showed that the protein has high homologs to pleurocidin-like peptide ( Pl p) from a fish Pleuronectus americanus. Moreover, the identified AMP is a cationic peptide with a good stability index, having a score of 31.50 predicted by the ProtParam. Therefore, the identified antimicrobial peptide ( Plp ) indicates that this cost-effective natural substance obtained from fish could potentially be used as a treatment for several bacterial and fungal infections in humans.
ISSN:1573-3904
1573-3149
1573-3904
DOI:10.1007/s10989-024-10589-8