Publisher: Elsevier BV

Issue: 21

License: https://www.elsevier.com/tdm/userlicense/1.0/

Publication date(s): 2018/11 (print)

Pages: 5691-5700

Volume: 26 Issue: 21

Journal: Bioorganic & Medicinal Chemistry

Link: https://api.elsevier.com/content/article/PII:S0968089618313233?httpAccept=text/xml

URL: http://dx.doi.org/10.1016/j.bmc.2018.10.015

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.