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An amphipathic cyclic tetrapeptide scaffold containing halogenated β2,2-amino acids with activity against multiresistant bacteria
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2018 (English)In: Journal of Peptide Science, ISSN 1075-2617, E-ISSN 1099-1387, Vol. 24, no 10, article id UNSP e3117Article in journal (Refereed) Published
Abstract [en]

The present study describes the synthesis and biological studies of a small series of head-to-tail cyclic tetrapeptides of the general structure c(Lys‐β2,2‐Xaa‐Lys) containing one lipophilic β2,2-amino acid and Lys, Gly, Ala, or Phe as the Xaa residue in the sequence. The peptides were investigated for antimicrobial activity against gram-positive and gram-negative reference strains and 30 multiresistant clinical isolates including strains with extended spectrum β-lactamase-carbapenemase (ESBL-CARBA) production. Toxicity was determined against human red blood cells. The most potent peptides showed high activity against the gram-positive clinical isolates with minimum inhibitory concentrations of 4-8μg/mL and low haemolytic activity. The combination of high antimicrobial activity and low toxicity shows that these cyclic tetrapeptides containing lipophilic β2,2-amino acids form a valuable scaffold for designing novel antimicrobial agents.

Place, publisher, year, edition, pages
John Wiley & Sons, 2018. Vol. 24, no 10, article id UNSP e3117
Keywords [en]
antimicrobial peptides, beta-amino acids, CARBA, cyclic tetrapeptides, ESBL, MRSA, multiresistant bacteria, peptidomimetics, SMAMPs, synthetic mimics of antimicrobial peptides
National Category
Medicinal Chemistry
Identifiers
URN: urn:nbn:se:umu:diva-153717DOI: 10.1002/psc.3117ISI: 000445732400005PubMedID: 30112781OAI: oai:DiVA.org:umu-153717DiVA, id: diva2:1266255
Available from: 2018-11-27 Created: 2018-11-27 Last updated: 2018-11-27Bibliographically approved

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Ochtrop, PhilippHedberg, Christian

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Bayer, AnnetteOchtrop, PhilippHedberg, ChristianHaug, TorStrøm, Morten B.
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  • apa
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