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Cover Picture: Chromophore‐Linked Substrate (CLS405): Probing Metallo‐β‐Lactamase Activity and Inhibition (ChemMedChem 12/2013)
Author(s) -
Makena Anne,
van Berkel Sander S.,
Lejeune Clarisse,
Owens Raymond J.,
Verma Anil,
Salimraj Ramya,
Spencer James,
Brem Jürgen,
Schofield Christopher J.
Publication year - 2013
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201390050
Subject(s) - chromogenic , chemistry , substrate (aquarium) , combinatorial chemistry , chromophore , stereochemistry , biology , chromatography , organic chemistry , ecology
The front cover picture shows the hydrolysis of chromogenic substrate CLS405 (green) by NDM‐1 (blue protein structure), a metallo‐beta‐lactamase (MBL), generating the detectable para ‐nitrophenolate product (yellow). Upon binding of an inhibitor ( N ‐hydroxythiazole shown in gray), hydrolysis of the substrate is hampered, thus facilitating rapid residual activity determination. Monitoring inhibition in a concentration‐dependent manner allows for straightforward IC 50 value determination using chromogenic substrate CLS405. Given the threat posed by MBLs to the clinical use of beta‐lactam antibiotics, the identification of MBL inhibitors is an important research goal. CLS405 represents a useful tool compound to facilitate the identification of improved MBL inhibitors with therapeutic potential against resistant strains of bacteria. For more details, see the Full Paper by Jürgen Brem, Christopher J. Schofield et al. on p. 1923 ff.