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Main Title: Extensive structure‐activity relationship study of albicidin’s C‐terminal dipeptidic p‐aminobenzoic acid moiety
Author(s): Behroz, Iraj
Durkin, Patrick
Grätz, Stefan
Seidel, Maria
Rostock, Lida
Spinczyk, Marcello
Weston, John B.
Süßmuth, Roderich D.
Type: Article
Language Code: en
Abstract: Albicidin is a recently described natural product that strongly inhibits bacterial DNA gyrase. The pronounced activity, particularly against Gram‐negative bacteria, turns it into a promising lead structure for an antibacterial drug. Hence, structure–activity relationship studies are key for the in‐depth understanding of structural features/moieties affecting gyrase inhibition, antibacterial activity and overcoming resistance. The 27 newly synthesized albicidins give profound insights into possibilities for variations of the C‐terminus. Furthermore, in the present study, a novel derivative has been identified as overcoming resistance posed by the Klebsiella‐protease AlbD. Structural modifications include, for example, azahistidine replacing the previous instable cyanoalanine as the central amino acid, as well as a triazole amide bond isostere between building blocks D and E.
Issue Date: 12-Dec-2019
Date Available: 13-Feb-2020
DDC Class: 540 Chemie und zugeordnete Wissenschaften
660 Chemische Verfahrenstechnik
Subject(s): Albicidin
drug discovery
natural products
structure–activity relationships
Sponsor/Funder: BMBF, 03VP00030, Validierung einer neuen antibakteriellen Wirkstoffklasse - AlbiPharm
TU Berlin, Open-Access-Mittel - 2019
Journal Title: Chemistry – A European Journal
Publisher: Wiley
Publisher Place: Weinheim
Volume: 25
Issue: 72
Publisher DOI: 10.1002/chem.201904752
Page Start: 16538
Page End: 16543
EISSN: 1521-3765
ISSN: 0947-6539
Appears in Collections:FG Biologische Chemie » Publications

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