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• W2108792803 abstract "ABSTRACT Human β-defensin 3 (hBD3) is a highly basic 45-amino-acid protein that acts both as an antimicrobial agent and as a chemoattractant molecule. Although the nature of its antimicrobial activity is largely electrostatic, the importance of the molecular structure on this activity is poorly understood. Two isoforms of hBD3 were synthesized: the first with native disulfide linkages and the second with nonnative linkages. In a third synthetic peptide, all cysteine residues were replaced with α-aminobutyric acid, creating a completely linear peptide. A series of six small, linear peptides corresponding to regions of hBD3 with net charges ranging from +4 to +8 (at pH 7) and lengths ranging from 9 to 20 amino acids were also synthesized. The linear full-length peptide showed the highest microbicidal activity against Escherichia coli and Staphylococcus aureus , while all three full-length forms showed equal activity against Candida albicans . The linear peptide also showed high activity against Enterococcus faecium and Pseudomonas aeruginosa. Peptides corresponding to the C terminus showed higher activities when tested against E. coli , with the most active peptides being the most basic. However, only the peptide corresponding to the N terminus of hBD3 showed any activity against S. aureus and C. albicans . Further, N-terminal deletion mutants of native hBD3 showed diminished activities against S. aureus . Thus, the antimicrobial properties of hBD3 derivatives are determined by both charge and structure." @default.
• W2108792803 created "2016-06-24" @default.
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• W2108792803 date "2003-09-01" @default.
• W2108792803 modified "2023-10-17" @default.
• W2108792803 title "Antimicrobial Characterization of Human β-Defensin 3 Derivatives" @default.
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• W2108792803 doi "https://doi.org/10.1128/aac.47.9.2804-2809.2003" @default.
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