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• W2060712617 abstract "We have developed a highly constrained 18-residue cyclic peptide template based on the antimicrobial peptide tachyplesin-1 that features an end-to-end peptide backbone and a cystine knot-like motif with three evenly spaced disulfide bonds to cross-brace the antiparallel β-strands and to approximate an amphiphatic “β-tile”-like structure. Six β-tile analogs were prepared to correlate different topological patterns with membranolytic specificity. Their conformations and antimicrobial and hemolytic activities were compared with tachyplesin-1 and the recently discovered Rhesus monkey theta defensin (RTD) which contains similar β-tile structural elements. The β-tile peptides and RTD retained broad spectrum antimicrobial activities. In general, they were less active than tachyplesin-1 in 10 tested organisms but their activity increased under high-salt (100 mM NaCl) rather than in low-salt conditions. The β-tile peptides are highly nontoxic to human erythrocytes with EC25 ranging from 600 to 4000 μM. Collectively, our results show that the design of a highly rigid peptide template is useful for further analog study to dissociate antimicrobial activity from cytotoxicity which would be helpful in discovering clinical applications for peptide antibiotics." @default.
• W2060712617 created "2016-06-24" @default.
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• W2060712617 date "2000-01-01" @default.
• W2060712617 modified "2023-09-30" @default.
• W2060712617 title "Marked Increase in Membranolytic Selectivity of Novel Cyclic Tachyplesins Constrained with an Antiparallel Two-β Strand Cystine Knot Framework" @default.
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• W2060712617 doi "https://doi.org/10.1006/bbrc.1999.2035" @default.
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