Chemical Modification of the Carboxyl Terminal of Nisin A with Biotin does not Abolish Antimicrobial Activity Against the Indicator Organism, Kocuria rhizophila |
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Authors: | Sam Maher Greg Vilk Fintan Kelleher Gilles Lajoie Siobhán McClean |
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Institution: | (1) Institute of Technology Tallaght Dublin (ITT Dublin) and National Institute of Cellular Biotechnology, Old Blessington Road, Tallaght, Dublin 24, Ireland;(2) Department of Biochemistry, University of Western Ontario, London, ON, Canada;(3) Present address: School of Agriculture, Food Science and Veterinary Medicine, University College Dublin, Belfield, Dublin 4, Ireland |
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Abstract: | Nisin is an antimicrobial peptide that is widely used for food preservation. Although it has potent activity against a number
of food pathogens, suggesting potential therapeutic applications, its potential for clinical use is limited by proteolytic
susceptibility and poor oral bioavailability. Derivatization of nisin could overcome these issues; however, many nisin analogues,
prepared by modification at the N-terminal and C-terminal have previously been shown to be inactive. A method for the C-terminal
modification was developed using biotinylation as a model derivative. Purification of the modified nisin was carried out using
reverse phase chromatography. Confirmation of nisin modification was confirmed by Mass Spectroscopy. The C-terminal modification
of nisin resulted in only a twofold reduction in antimicrobial activity of the conjugate against the indicator organism, Kocuria rhizophila. The C-terminal modification could be used to increase the therapeutic potential of nisin by creating more favourable physicochemical
characteristics. This is the first study that showed that nisin modification can be carried out successfully without destroying
its antimicrobial activity. |
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Keywords: | Nisin Antimicrobial peptide Biotinylation C-terminal modification Therapeutic application |
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