Novel temporin L antimicrobial peptides: promoting self-assembling by lipidic tags to tackle superbugs. (1st January 2020)

• Record Type: Journal Article
• Authors: Bellavita, Rosa; Falanga, Annarita; Buommino, Elisabetta; Merlino, Francesco; Casciaro, Bruno; Cappiello, Floriana; Mangoni, Maria Luisa; Novellino, Ettore; Catania, Maria Rosaria; Paolillo, Rossella; Grieco, Paolo; Galdieroa, Stefania
• Is Part Of: Journal of enzyme inhibition and medicinal chemistry. Volume 35:Number 1(2020)
• Page Start: 1751
• Page End: 1764
• Publication Date: 2020-01-01
• Subjects: Antimicrobial peptides (AMPs) -- temporin L analogues -- self-assembling -- membrane interaction; Enzyme inhibitors -- Periodicals; Enzyme Inhibitors -- periodicals; Biochemistry -- periodicals; 572.7
• DOI: 10.1080/14756366.2020.1819258
• Languages: English
• ISSNs: 1475-6366

Abstract

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.