Abstract
Lantibiotics form a particular group within the antibiotic peptides and are distinguished by several features such as primary and spatial structure peculiarities, unprecedented peptide modification reactions, unique biosynthetic pathways and potent antibacterial activity.1 These properties have attracted much interest over the last decade from both basic researchers of various disciplines and applied sciences aiming at introducing such peptides into agro-food and biomedical industries. Indeed, nisin, the most prominent and best studied lantibiotic, has a long and well documented history as an effective and safe food preservative.2 The success of nisin induced enormous research efforts from dairy and food industries, and these efforts have in turn led to a wealth of information on the biosynthesis, molecular genetics and structure-function relationships of lantibiotics and related unmodified peptide bacteriocins.3 Although lantibiotics in many ways are unique peptides, they should not be regarded as a separate entity, but rather be discussed in context with antibiotic peptides in general.
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Jack, R.W., Bierbaum, G., Sahl, HG. (1998). Antimicrobial Peptides. In: Lantibiotics and Related Peptides. Biotechnology intelligence unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-08239-3_1
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DOI: https://doi.org/10.1007/978-3-662-08239-3_1
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