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.
Keywords:
Antimicrobial peptide; Bioconjugates; Cationic peptide; Lantibiotics; Peptoid.
Copyright © 2018 The Authors. Published by Elsevier Ltd.. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Bacterial Agents / chemical synthesis
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Anti-Bacterial Agents / chemistry
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Anti-Bacterial Agents / pharmacology*
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Antimicrobial Cationic Peptides / chemical synthesis
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Antimicrobial Cationic Peptides / chemistry
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Antimicrobial Cationic Peptides / pharmacology*
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Bacillus subtilis / drug effects
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Escherichia coli / drug effects
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Micrococcus luteus / drug effects
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Nisin / analogs & derivatives*
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Nisin / chemical synthesis
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Nisin / pharmacology*
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / pharmacology*
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Peptoids / chemical synthesis
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Peptoids / chemistry
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Peptoids / pharmacology*
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Pseudomonas aeruginosa / drug effects
Substances
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Anti-Bacterial Agents
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Antimicrobial Cationic Peptides
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Peptide Fragments
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Peptoids
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Nisin