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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Cerofolini L, Amato J, Borsi V, Pagano B, Randazzo A, and Fragai M
- Subjects
- Binding Sites, Humans, Ligands, Models, Molecular, Protein Binding, Protein Structure, Tertiary, Distamycins chemistry, S100 Calcium Binding Protein beta Subunit chemistry
- 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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