1. Probing the interaction of distamycin A with S100β: the 'unexpected' ability of S100β to bind to DNA-binding ligands
- Author
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Linda Cerofolini, Marco Fragai, Valentina Borsi, Bruno Pagano, Antonio Randazzo, and Jussara Amato
- Subjects
chemistry.chemical_classification ,Stereochemistry ,Lexitropsin ,Nuclear magnetic resonance spectroscopy ,In vitro ,DNA sequencing ,chemistry.chemical_compound ,chemistry ,Biochemistry ,Structural Biology ,Docking (molecular) ,Non-covalent interactions ,DISTAMYCIN A ,Molecular Biology ,DNA - Abstract
DNA-minor-groove-binding ligands are potent antineoplastic molecules. The antibiotic distamycin A is the prototype of one class of these DNA-interfering molecules that have been largely used in vitro. The affinity of distamycin A for DNA is well known, and the structural details of the complexes with some B-DNA and G-quadruplex-forming DNA sequences have been already elucidated. Here, we show that distamycin A binds S100β, a protein involved in the regulation of several cellular processes. The reported affinity of distamycin A for the calcium(II)-loaded S100β reinforces the idea that some biological activities of the DNA-minor-groove-binding ligands arise from the binding to cellular proteins. Copyright © 2015 John Wiley & Sons, Ltd.
- Published
- 2015
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