Activity and Export of Engineered Nisin-(1-22) Analogs

Polymers

Annechien Plat²  Anneke Kuipers²  Jacobien G. de Lange²  Gert N. Moll¹ 

[1] BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands;

关键词: nisin;    lantibiotic;    peptide;    cyclization;    Lactococcus;   

DOI  :  10.3390/polym3031282

来源: mdpi

【 摘 要 】

The pentacyclic peptide antibiotic nisin, produced by Lactococcus lactis is ubiquitously applied as a food preservative. We previously demonstrated that the truncated nisin-(1-22) has only 10-fold lower activity than nisin. Here we aimed at further developing this tricyclic nisin analog to reach activity comparable to that of nisin. Our data demonstrate that: (1) ring A has a large mutational freedom; (2) the composition of residues 20–22 strongly affects production levels of nisin-(1-22); (3) a positively charged C-terminus of nisin-(1-22) significantly enhances its antimicrobial activity; (4) nisin-(1-22) inhibits in vitro growth of a target strain using different dynamics than nisin.

【 授权许可】

CC BY   
© 2011 by the authors; licensee MDPI, Basel, Switzerland.