Mitchell, SA;
Truscott, F;
Dickman, R;
Ward, J;
Tabor, AB;
(2018)
Simplified lipid II-binding antimicrobial peptides: Design, synthesis and antimicrobial activity of bioconjugates of nisin rings A and B with pore-forming peptides.
Bioorganic & Medicinal Chemistry
, 26
(21)
pp. 5691-5700.
10.1016/j.bmc.2018.10.015.
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Abstract
New designs of antimicrobial peptides are urgently needed in order to combat the threat posed by the recent increase of resistance to antibiotics. In this paper, we present a new series of antimicrobial peptides, based on the key structural features of the lantibiotic nisin. We have simplified the structure of nisin by conjugating the lipid II-binding motif at the N-terminus of nisin to a series of cationic peptides and peptoids with known antibacterial action and pore-forming properties. Hybrid peptides, where a hydrophilic PEG4 linker was used, showed good antibacterial activity against Micrococcus luteus.
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