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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 [J Enzyme Inhib Med Chem] 2020 Dec; Vol. 35 (1), pp. 1751-1764. - Publication Year :
- 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.
- Subjects :
- Animals
Anti-Bacterial Agents chemical synthesis
Anti-Bacterial Agents chemistry
Antimicrobial Cationic Peptides chemical synthesis
Antimicrobial Cationic Peptides chemistry
Cell Survival drug effects
Cells, Cultured
Dose-Response Relationship, Drug
Humans
Microbial Sensitivity Tests
Molecular Structure
Proteolysis drug effects
Sheep
Structure-Activity Relationship
Anti-Bacterial Agents pharmacology
Antimicrobial Cationic Peptides pharmacology
Klebsiella pneumoniae drug effects
Pseudomonas aeruginosa drug effects
Staphylococcus aureus drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 1475-6374
- Volume :
- 35
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of enzyme inhibition and medicinal chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 32957844
- Full Text :
- https://doi.org/10.1080/14756366.2020.1819258