Title | Investigation of the interaction of "core" 2′,5′-oligoadenylates with some proteins by fluorescence spectroscopy |
Publication Type | Journal Article |
Year of Publication | 2015 |
Authors | Tkachuk, VV, Levchenko, SM, Rebriev, AV, Tkachuk, LV, Chernykh, SI, Tkachuk, ZYu. |
Abbreviated Key Title | Dopov. Nac. akad. nauk Ukr. |
DOI | 10.15407/dopovidi2015.02.158 |
Issue | 2 |
Section | Biochemistry |
Pagination | 158-164 |
Date Published | 2/2015 |
Language | Ukrainian |
Abstract | The interactions between "core" oligoadenylates (2′,5′-A3) and its analogs with albumin, interferon, insulin, immunoglobulin, and calmodulin are studied, by using fluorescence spectroscopy and mass spectrometry. It is shown that all oligoadenylates quench the intrinsic fluorescence of these proteins in varying degrees. Quenching degree depends on the olygoadenylates concentration. 2′,5′-A3 and its analogs 2′,5′-A3-thio, 2′,5′-A3-ino, and 2′,5′-A3-cord substantially quench the proteins fluorescence excited at a wavelength of 280 nm and do significantly less at an excitation wavelength of 296 nm that may indicate the possible tyrosine role in the binding of these drugs to proteins. At the same time, in the case of 2′,5′-A3-epo and 2′,5′-A3-NH2, their interaction with proteins can occur via tyrosine and tryptophan, as there is a significant increase in the proteins fluorescence quenching at an excitation wavelength of 296 nm, especially for 2′,5′-A3-NH2. Possible mechanisms of interaction between the investigated proteins and oligoadenylates are under discussion. |
Keywords | albumin, analog, core oligoadenylate, fluorescence spectroscopy, oligoadenylate |
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