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Activity and Export of Engineered Nisin-(1-22) Analogs
BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Groningen, The Netherlands
* Author to whom correspondence should be addressed.
Received: 4 July 2011; in revised form: 29 July 2011 / Accepted: 11 August 2011 / Published: 12 August 2011
Abstract: 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
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MDPI and ACS Style
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.
Plat A, Kuipers A, Lange JG, Moll GN, Rink R. Activity and Export of Engineered Nisin-(1-22) Analogs. Polymers. 2011; 3(3):1282-1296.
Plat, Annechien; Kuipers, Anneke; Lange, Jacobien G. de; Moll, Gert N.; Rink, Rick. 2011. "Activity and Export of Engineered Nisin-(1-22) Analogs." Polymers 3, no. 3: 1282-1296.