Yes / 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. / Engineering and Physical Sciences Research Council (EPSRC) and Yorkshire Cancer Research
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/8900 |
| Date | 06 May 2016 |
| Creators | Sellars, J.D., Skipsey, M., Sadr-ul-Shaheed, Gravell, Sebastian, Abumansour, Hamza M.A., Kashtl, Ghasaq J., Irfan, Jawaria, Khot, Ibrahim, Pors, Klaus, Patterson, Laurence H., Sutton, Chris W. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, Accepted manuscript |
| Rights | (c) Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer-reviewed version of the following article: Sellars JD, Skipsey M, Sadr-ul-Shaheed S et al (2016) Rational development of novel activity probes for the analysis of human cytochromes P450. ChemMedChem. 11(11): 1122-1128, which has been published in final form at http://dx.doi.org/10.1002/cmdc.201600134. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. |
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