6qxb

NMR structure of peptide 7, characterized by a cis-4-amino-Pro residue, with a significant lower MIC on E. coli

spinqualitylabelsall models 6qxb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qxb is a 1 chain structure with sequence from Pseudis bolbodactyla. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: JKH, NH2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Previously, we identified a potent antimicrobial analogue of temporin L (TL), [Pro3]TL, in which glutamine at position 3 was substituted with proline. In this study, a series of analogues, where the position 3 was substituted with non-natural proline derivatives, was investigated for the correlation between the conformational properties of the compounds and their antibacterial, cytotoxic and hemolytic activities. Non-natural proline analogues with substituents at position 4 of the pyrrolidine ring were considered. Structure-activity relationship studies of these analogues were performed by means of antimicrobial and cytotoxicity assays along with circular dichroism (CD) and NMR spectroscopy analysis for selected compounds. The most promising peptides were additionally evaluated for their activity against some representative veterinary microbial strains to compare with those from human strains. We identified novel analogues with interesting properties that make them attractive lead compounds. The Outcomes of Decorated-Prolines in Discovering Novel Antimicrobial Peptides from Temporin-L.,Grieco P, Buommino E, Carotenuto A, Antignano I, Bellavita R, Casciaro B, Loffredo MR, Merlino F, Novellino E, Mangoni ML, Nocera FP, Brancaccio D, Punzi P, Roversi D, Ingenito R, Bianchi E ChemMedChem. 2019 May 14. doi: 10.1002/cmdc.201900221. PMID:31087626 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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