Title: Simplified lipid II-binding antimicrobial peptides: Design, synthesis and antimicrobial activity of bioconjugates of nisin rings A and B with pore-forming peptides

Authors (5): S. A. Mitchell, F. Truscott, R. Dickman, J. Ward, A. B. Tabor

Themes: Biocatalysis (2018)

DOI: 10.1016/j.bmc.2018.10.015

Citations: 14

Pub type: article-journal

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.

Name Description Publised
1-s2.0-S0968089618313233-mmc1.docx Supl. data for Simplified lipid II-binding antimicrobial peptides: Desig... 2018


Back