%0 Journal Article
%T Studies on interaction of oligoadenylates with proteins in vitro by MALDI-TOF mass spectrometry
%A Levchenko S. M.
%A Rebriev A. V.
%A Tkachuk V. V.
%A Dubey L. V.
%J Biopolymers and Cell
%D 2013
%I Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine
%R 10.7124/bc.000804
%X Aim. To investigate the ability of  core  2'-5'- and 3'-5'-oligoadenylates (OA) to interact with ¦Á-interferon ¨C a key protein of the 2'- 5'-OAS/RNAase L system responsible for antiviral cell defense. Methods. MALDI-TOF mass spectrometry was used in the studies on protein-ligand interactions. Results. It was shown that 2'-5'-§¡3 and its epoxy-modified analog 2'-5'-§¡3-epo can bind to ¦Á-interferon in vitro. 3'-5'-tri- adenylate is also capable of binding to this protein. One to five ligand molecules can bind simultaneously to the molecule of ¦Á-interferon. At the same time, all studied oligonucleotides do not bind to insulin. Conclusions. It was established that  core  2'-5'- and 3'-5'-triadenylates are capable of multiple interaction with ¦Á-interferon to form stable complexes. However, they do not bind to insulin which is not involved in the 2'-5'-OAS/RNAase L system.
%K oligoadenylates
%K insulin
%K ¦Á-interferon
%K MALDI-TOF mass spectrometry
%U http://biopolymers.org.ua/pdf/uk/29/1/042/