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Polymers 2011, 3(3), 1282-1296; doi:10.3390/polym3031282

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

*  and
BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands
* Author to whom correspondence should be addressed.
Received: 4 July 2011 / Revised: 29 July 2011 / Accepted: 11 August 2011 / Published: 12 August 2011
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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.
Keywords: nisin; lantibiotic; peptide; cyclization; Lactococcus nisin; lantibiotic; peptide; cyclization; Lactococcus
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Plat, A.; Kuipers, A.; Lange, J.G.; Moll, G.N.; Rink, R. Activity and Export of Engineered Nisin-(1-22) Analogs. Polymers 2011, 3, 1282-1296.

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