Optical Response of the Polynucleotides-Proteins Interaction

The optical absorption, fluorescence, and phosphorescence spectra of RNAs and oligonucleotides of different origin, as well as their mixtures with human albumin are investigated. It is confirmed that the energy structures of DNA, RNA, and complex protein macromolecules are determined mainly by the i...

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Bibliographic Details
Published in:Molecular Crystals and Liquid Crystals 2011-03, Vol.535 (1), p.93-110
Main Authors: Yashchuk, Valeriy M., Kudrya, Vladislav Yu, Levchenko, Svitlana M., Tkachuk, Zenoviy Yu, Hovorun, Dmytro M., Mel'nik, Volodymyr I., Vorob'yov, Volodymyr P., Klishevich, Georgiy V.
Format: Article
Language:English
Subjects:
Albumins
Binding
Binding sites
Deoxyribonucleic acid
DNA
Electrons
Energy levels
Fluorescence
Human
Human albumin
Macromolecules
Molecular structure
Molecules
oligoadenylate
Oligonucleotides
Phosphorescence
Polynucleotides
Proteins
Ribonucleic acid
Ribonucleic acids
RNA
Spectra
Spectrum analysis
Studies
triplet excitations
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Summary:The optical absorption, fluorescence, and phosphorescence spectra of RNAs and oligonucleotides of different origin, as well as their mixtures with human albumin are investigated. It is confirmed that the energy structures of DNA, RNA, and complex protein macromolecules are determined mainly by the individual properties of their π-electron systems. The positions of the RNA excited singlet and triplet energy levels obtained by authors' previous work are determined more precisely. It is shown that mainly adenine bases are traps for mobile triplet excitons in RNA (contrary to DNA, in which AT complexes are the triplet traps). The spectral manifestation of the RNA/oligonucleotides-albumin interaction is studied. It turns out that namely the phosphorescence spectra of these compounds due to their sharp structure at 4.2 K are the most suitable for the study of the RNA-albumin interaction. The phosphorescence spectra of albumin-2′5′A 3 solvents manifest the penetrative binding of 2′5′A 3 to an albumin macromolecule. The obtained data show that at least a weak non-penetrative binding of RNA to human albumin can exist.
ISSN:1542-1406
1563-5287
1527-1943
DOI:10.1080/15421406.2011.537953