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Frog Skin Peptide Neutralises MRSA in Preclinical Tests

Neo Science Hub by Neo Science Hub
1 month ago
in Healthcare & Medicine, Blogs, Research & Development, Science News
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Frog Skin Peptide Neutralises MRSA in Preclinical Tests
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A novel antimicrobial peptide isolated from the Yunnanfu frog has demonstrated potent activity against methicillin-resistant Staphylococcus aureus (MRSA), offering a promising lead in the fight against antibiotic-resistant superbugs. The peptide, named brevinin-1E-OG9, was extracted from skin secretions of Odorrana grahami and has shown remarkable efficacy in both laboratory and skin infection models.

Researchers identified the compound through “shotgun” cloning of frog skin secretion-derived cDNA, revealing a precursor that encodes the 24-amino-acid peptide. The mature peptide features a distinctive “Rana Box” structure—a cyclic heptapeptide at the C-terminus that is characteristic of the brevinin-1 family and appears critical for antimicrobial activity. In vitro testing confirmed that brevinin-1E-OG9 rapidly disrupts bacterial cell membranes, with particular potency against S. aureus strains, including MRSA.

The study team, led by scientists at Queen’s University Belfast, went further by designing analogues to optimise the peptide’s therapeutic profile. One modified version, brevinin-1E-OG9c-De-NH₂, exhibited enhanced antimicrobial efficacy and reduced inflammatory responses in ex vivo porcine skin models. This analogue not only killed bacteria but also attenuated inflammation triggered by bacterial lipoteichoic acid, suggesting dual antibacterial and immunomodulatory benefits.

The significance extends beyond a single peptide. With over 1,000 antimicrobial peptides (AMPs) identified in amphibians worldwide, frogs represent an evolutionary treasure trove of molecular disinfectants. These peptides have co-evolved over millions of years to protect amphibians from pathogens in their microbe-rich aquatic environments, making them inherently robust against resistance development. Unlike conventional antibiotics that target specific bacterial enzymes, AMPs work by physically disrupting microbial membranes—a mechanism that makes resistance far less likely to emerge.

The research team emphasises that brevinin-1E-OG9 is still in preclinical development, requiring extensive safety testing before human trials can be considered. However, the work validates a systematic approach: screen amphibian biodiversity, identify lead compounds, then engineer analogues with improved selectivity and reduced toxicity. As antibiotic resistance accelerates globally, the humble frog’s skin may prove more valuable than any synthetic library.

– Dr. Siva SR Pakanati

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Tags: featuredNewsHub Jan 26sciencenewsWild Healers
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