A Review on Bioactive Porcine Peptide, Protegrin-1
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Multi drug resistance is a major problem of the twenty first century. In order to combat this issue, there is an urgent need in the pharmaceutical industry, for novel therapeutic agents. Antimicrobial peptides such as protegrins which exhibit non-specific membranolytic action can be viewed as probable therapeutic agents and replace conventional antibiotics. Protegrin-1 (PG-1) is a peptide isolated from porcine leucocytes. Its primary role is its antimicrobial activity against a broad-spectrum of gram-positive as well as gram-negative bacteria and fungi. Its antagonistic activity can be accounted by its pore formation mechanism in microbial membranes. In addition, PG-1 has multiple roles viz., anticancer and antiviral activity, immunomodulatory functions and numerous applications which increase its suitability as a potential therapeutic agent. This review paper presents a comprehensive overview of biological roles, lytic mechanism of action and applications of PG-1, thus providing a thorough understanding of this β-sheet peptide, which structurally resembles defensin peptides.
KeywordsMulti-drug resistance Therapeutic agent Antimicrobial peptides Protegrin-1
Atomic force microscopy
Grazing incidence X-ray diffraction
Nuclear magnetic resonance
Oriented circular dichroism
World Health Organization
The authors thank Vellore Institute of Technology (Deemed to be University) for providing ‘VIT SEED GRANT’ for carrying out this review on protegrin-1.
Conceptualization: [RR]; Literature survey, data analysis and drafting the article: [SSR]; Critical revision of article: [RR].
Compliance with Ethical Standards
Conflict of interest
The authors declare that they have conflict of interest.
Informed consent was obtained from all individual participants included in the study.
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