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 p-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 0 5 0 A 3 solvents manifest the penetrative binding of 2 0 5 0 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.
The influenza virus hemagglutinin (HA) mediates both receptor (glycan) binding and membrane fusion for cell entry and has been the basis for subtyping influenza viruses. The oligoribonucleotides-d-mannitol (ORNs-d-M) complexes possess an anti-influenza activity in vitro and in vivo. In the present studies, we have found that ORNs-d-M interferes with hemagglutinin (HA)–glycan interaction and suppress viral infection in host cells. HA–glycan interactions were evaluated to indirectly quantify the amount of influenza virus titer by an agglutination assay. Influenza virus infectivity was determined by TCID50 assay. The direct virucidal action of the complexes was evaluated by both cytopathic effects (CPE) reduction assay and cell MTT assay. We found that ORNs-d-M hinders interaction between HA and glycan. These complexes decreased the infectivity of influenza virus and had a direct virucidal action. ORNs-d-M reduces influenza virus infectivity, affecting the HA–glycan interaction in vitro. By suppressing the influenza viral infection, the ORNs-d-M can have direct virucidal action.
It has been shown that nu cleic ac ids re veal mem brane-sta bi liz ing and anti-in flam ma tory ac tions de pend ing on the or i gin and the pu rity level in in vi tro and in vivo ex per i ments. The pu ri fied yeast RNA has been found to be the most ef fec tive.
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