Rational Development of Novel Activity Probes for the Analysis of Human Cytochromes P450

Autor:	Hamza Abumansour, Sadr-ul-Shaheed, Jonathan D. Sellars, Laurence H. Patterson, Mark Skipsey, Sebastian Gravell, Ghasaq Kashtl, Klaus Pors, Chris W. Sutton, Mohamed Khot, Jawaria Irfan
Rok vydání:	2016
Předmět:	Proteomics 0301 basic medicine Gene isoform Immunoblotting urologic and male genital diseases 01 natural sciences Biochemistry Mass Spectrometry 03 medical and health sciences Cytochrome P-450 Enzyme System Drug Discovery Humans Protein Isoforms heterocyclic compounds General Pharmacology Toxicology and Pharmaceutics Benzofurans Pharmacology chemistry.chemical_classification biology 010405 organic chemistry organic chemicals Organic Chemistry Cytochrome P450 respiratory system 0104 chemical sciences Protein profiling Kinetics enzymes and coenzymes (carbohydrates) 030104 developmental biology Enzyme Liver chemistry Molecular Probes biology.protein Molecular Medicine NADP Protein Binding
Zdroj:	ChemMedChem, 2016, Vol.11(11), pp.1122-1128 [Peer Reviewed Journal]
ISSN:	1860-7179
Popis:	The identification and quantification of functional cytochromes P450 (CYPs) in biological samples is proving important for robust analyses of drug efficacy and metabolic disposition. In this study, a novel CYP activity-based probe was rationally designed and synthesised, demonstrating selective binding of CYP isoforms. The dependence of probe binding upon the presence of NADPH permits the selective detection of functionally active CYP. This allows the detection and analysis of these enzymes using biochemical and proteomic methodologies and approaches.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::470b2d4d8f2738bea40bd4b51bfa8469 https://doi.org/10.1002/cmdc.201600134 Zobrazit plný text záznamu Plný text