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Design and evaluation of tadpole-like conformational antimicrobial peptides.
- Source :
-
Communications biology [Commun Biol] 2023 Nov 18; Vol. 6 (1), pp. 1177. Date of Electronic Publication: 2023 Nov 18. - Publication Year :
- 2023
-
Abstract
- Antimicrobial peptides are promising alternatives to conventional antibiotics. Herein, we report a class of "tadpole-like" peptides consisting of an amphipathic α-helical head and an aromatic tail. A structure-activity relationship (SAR) study of "tadpole-like" temporin-SHf and its analogs revealed that increasing the number of aromatic residues in the tail, introducing Arg to the α-helical head and rearranging the peptide topology dramatically increased antimicrobial activity. Through progressive structural optimization, we obtained two peptides, HT2 and RI-HT2, which exhibited potent antimicrobial activity, no hemolytic activity and cytotoxicity, and no propensity to induce resistance. NMR and molecular dynamics simulations revealed that both peptides indeed adopted "tadpole-like" conformations. Fluorescence experiments and electron microscopy confirmed the membrane targeting mechanisms of the peptides. Our studies not only lead to the discovery of a series of ultrashort peptides with potent broad-spectrum antimicrobial activities, but also provide a new strategy for rational design of novel "tadpole-like" antimicrobial peptides.<br /> (© 2023. The Author(s).)
Details
- Language :
- English
- ISSN :
- 2399-3642
- Volume :
- 6
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Communications biology
- Publication Type :
- Academic Journal
- Accession number :
- 37980400
- Full Text :
- https://doi.org/10.1038/s42003-023-05560-0