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Novel temporin L antimicrobial peptides: promoting self-assembling by lipidic tags to tackle superbugs
- Source :
- Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 35, Iss 1, Pp 1751-1764 (2020)
- Publication Year :
- 2020
- Publisher :
- Taylor & Francis Group, 2020.
-
Abstract
- The rapid development of antimicrobial resistance is pushing the search in the discovering of novel antimicrobial molecules to prevent and treat bacterial infections. Self-assembling antimicrobial peptides, as the lipidated peptides, are a novel and promising class of molecules capable of meeting this need. Based on previous work on Temporin L analogs, several new molecules lipidated at the N- or and the C-terminus were synthesised. Our goal is to improve membrane interactions through finely tuning self-assembly to reduce oligomerisation in aqueous solution and enhance self-assembly in bacterial membranes while reducing toxicity against human cells. The results here reported show that the length of the aliphatic moiety is a key factor to control target cell specificity and the oligomeric state of peptides either in aqueous solution or in a membrane-mimicking environment. The results of this study pave the way for the design of novel molecules with enhanced activities.
Details
- Language :
- English
- ISSN :
- 14756366 and 14756374
- Volume :
- 35
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Journal of Enzyme Inhibition and Medicinal Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.fbb519ebab4547f6a5bf64777c38cefb
- Document Type :
- article
- Full Text :
- https://doi.org/10.1080/14756366.2020.1819258