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Z. Naturforsch. 69a, 331 – 338
(2014)
doi:10.5560/ZNA.2014-0021
Computational Study of the Structure, the Flexibility, and the Electronic Circular Dichroism of Staurosporine – a Powerful Protein Kinase Inhibitor
Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne, NE1 8ST, United Kingdom
Received January 6, 2014 / revised February 28, 2014 / published online July 15, 2014
Reprint requests to: C. Z. C.; E-mail:
christo.christov@northumbria.ac.uk
Staurosporine (STU) is a microbial alkaloid which is an universal kinase inhibitor. In order to understand its mechanism of action it is important to explore its structure-properties relationships. In this paper we provide the results of a computational study of the structure, the chiroptical properties, the conformational flexibility of STU as well as the correlation between the electronic circular dichroism (ECD) spectra and the structure of its complex with anaplastic lymphoma kinase.
Key words: Staurosporine; Computational Chemistry; Electronic Circular; Dichroism; Molecular Dynamics; Anaplastic Lymphoma Kinase.