Work

A truncated nisin variant, lipidated at its C-terminus, displays improved stability and increased antibacterial activity against methicillin-resistant Staphylococcus aureus

Year: 2026

Type: article

Abstract: . Notably, due to its short length, ring-protected structure, and lipid modification, the construct demonstrated improved proteolytic stability against chymotrypsin, trypsin and protease K. Our findings suggest that optimizing lipid-peptide combinations can lead to more effective, specific, and stable candidates for antimicrobial development.

Source: RSC Chemical Biology

DOI: 10.1039/d6cb00193a

Authors: Longcheng Guo, Chenhui Wang, Oscar P. Kuipers, Jaap Broos

Institutions: University of Groningen, University of Hong Kong

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $1,962