Studies on interaction of oligoadenylates with proteins in vitro by MALDI-TOF mass spectrometry

Aim. To investigate the ability of «core» 2'-5'- and 3'-5'-oligo- adenylates (OA) to interact with -interferon –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-li- gand interactions. Results. It was shown that 2'-5'-A3 and its epoxy-modified analog 2'-5'-A3 -epo can bind to-interferon in vitro. 3'-5'-triadenylate is also capable of binding to this protein. One to five ligand molecules can bind simultaneously to the molecule of -interferon. At the same time, all studied oligonucleotides do not bind to insulin. Con- clusions. It was established that «core» 2'-5'- and 3'-5'-triadenylates are capable of multiple interaction with -interferon to form stable complexes. However, they do not bind to insulin which is not involved in the 2'-5'-OAS/RNAase L system.