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• W2046740017 abstract "ABSTRACT Caseicins A and B are low-molecular-weight antimicrobial peptides which are released by proteolytic digestion of sodium caseinate. Caseicin A (IKHQGLPQE) is a nine-amino-acid cationic peptide, and caseicin B (VLNENLLR) is a neutral eight-amino-acid peptide; both have previously been shown to exhibit antibacterial activity against a number of pathogens, including Cronobacter sakazakii . Previously, four variants of each caseicin which differed subtly from their natural counterparts were generated by peptide synthesis. Antimicrobial activity assays revealed that the importance of a number of the residues within the peptides was dependent on the strain being targeted. In this study, this engineering-based approach was expanded through the creation of a larger collection of 26 peptides which are altered in a variety of ways. The investigation highlights the generally greater tolerance of caseicin B to change, the fact that changes have a more detrimental impact on anti-Gram-negative activity, and the surprising number of variants which exhibit enhanced activity against Staphylococcus aureus ." @default.
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• W2046740017 date "2012-01-13" @default.
• W2046740017 modified "2023-09-23" @default.
• W2046740017 title "Extensive Manipulation of Caseicins A and B Highlights the Tolerance of These Antimicrobial Peptides to Change" @default.
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• W2046740017 doi "https://doi.org/10.1128/aem.07312-11" @default.
• W2046740017 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3302613" @default.
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