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Manipulating turn residues on de novo designed β-hairpin peptides for selectivity against drug-resistant bacteria

Acta Biomater. 2021-09; 
Nhan D T Tram, Vanitha Selvarajan, Alister Boags, Devika Mukherjee, Jan K Marzinek, Bernadette Cheng, Zi-Chen Jiang, Pascal Goh, Jun-Jie Koh, Jeanette W P Teo, Peter J Bond, Pui Lai Rachel Ee
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摘要

Synthetic β-hairpin antimicrobial peptides (AMPs) offer a useful source for the development of novel antimicrobial agents. β-hairpin peptides generally consist of two side strands bridged by a reverse turn. In literature, most studies focused on the modifications of the side strands to manipulate the stability and activity of β-hairpin peptides, and much less is known about the impact of the turn region. By designing a series of de novo β-hairpin peptides with identical side strands but varied turns, we demonstrated that mutations of only 2 to 4 amino acids at the turn region could impart a wide range of antimicrobial profiles among synthetic β-hairpin AMPs. BTT2-4 and BTT6 displayed selective potency agai... More

关键词

Antimicrobial peptide, Colistin resistance, Gram-negative bacteria, Selective activity, β-hairpin