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Raman and surface‐enhanced Raman scattering spectroscopy of bis‐netropsins and their DNA complexes
Author(s) -
Ermishov Mikhail,
Sukhanova Alyona,
Kryukov Evgeniy,
Grokhovsky Sergei,
Zhuze Alexei,
Oleinikov Vladimir,
Jardillier Jean Claude,
Nabiev Igor
Publication year - 2000
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/1097-0282(2000)57:5<272::aid-bip40>3.0.co;2-v
Subject(s) - chemistry , dna , raman spectroscopy , binding constant , enzyme , crystallography , stereochemistry , binding site , biochemistry , physics , optics
The interactions of three bis‐netropsins (bis‐Nts), which are potent catalytic inhibitors of DNA‐binding enzymes, with three double‐stranded oligonucleotides (OLIGs), which contain sites of different specific affinities for each bis‐Nt, were analyzed. Raman spectroscopy was performed for selective monitoring of modifications of the bis‐Nt or the OLIG structure upon bis‐Nt–DNA binding, and surface‐enhanced Raman scattering spectroscopy (SERS) was an additional tool for topology studies of ligand–DNA complexes. The spectral data showed conformational changes of both partners (bis‐Nt and OLIG) upon complexation. Structural variations of bis‐Nts appeared to be dependent on a bis‐Nt–OLIG binding constant and were found to be small in the specific DNA binding and highest for nonspecific binding of bis‐Nt with the corresponding OLIG. The conformational changes of the OLIGs were varied with a bis‐Nt–OLIG binding constant in the same manner. The bis‐Nts seemed to induce a perturbation in the OLIG's structure, as well as in the positions of their direct binding. These DNA structural modification effects may explain the inhibition of DNA‐binding enzymes in the variety of very distinct DNA–enzyme binding sites by bis‐Nts reported previously. © 2000 John Wiley & Sons, Inc. Biopolymers (Biospectroscopy) 57: 272–281, 2000