Biopolym. Cell. 2013; 29(1):42-48.
http://dx.doi.org/10.7124/bc.000804
Structure and Function of Biopolymers
Studies on interaction of oligoadenylates with proteins in vitro by MALDI-TOF mass spectrometry
1Levchenko S. M., 2Rebriev A. V., 1Tkachuk V. V., 1Dubey L. V., 1Dubey I. Ya., 1Tkachuk Z. Yu.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
  2. Palladin Institute of Biochemistry, NAS of Ukraine
    9, Leontovycha Str., Kyiv, Ukraine, 01601

Abstract

Aim. To investigate the ability of «core» 2'-5'- and 3'-5'-oligoadenylates (OA) to interact with α-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-ligand interactions. Results. It was shown that 2'-5'-A3 and its epoxy-modified analog 2'-5'-A3-epo can bind to α-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 α-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 α-interferon to form stable complexes. However, they do not bind to insulin which is not involved in the 2'-5'-OAS/RNAase L system.
Keywords: oligoadenylates, insulin, α-interferon, MALDI-TOF mass spectrometry
Full text: (PDF, in English) (PDF, in Ukrainian)

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