Interaction between thrombin and oligonucleotide RA36 is a two-stage process

Olga M Antipova; Georgy M Solius; Dmitry Y Panteleev; Roman V Reshetnikov

doi:10.1016/j.bbrc.2019.11.190

Interaction between thrombin and oligonucleotide RA36 is a two-stage process

Biochem Biophys Res Commun. 2020 Feb 19;522(4):1037-1040. doi: 10.1016/j.bbrc.2019.11.190. Epub 2019 Dec 6.

Authors

Olga M Antipova¹, Georgy M Solius², Dmitry Y Panteleev³, Roman V Reshetnikov⁴

Affiliations

¹ Apto-Pharm Ltd, Kolomensky dr., 13A, 115564, Moscow, Russia; Chemistry Department, Lomonosov Moscow State University, Leninskie Gory 1-40, 119991, Moscow, Russia. Electronic address: antipovachem@gmail.com.
² Apto-Pharm Ltd, Kolomensky dr., 13A, 115564, Moscow, Russia; Institute of Gene Biology, Russian Academy of Sciences, Vavilova str., 34/5, 119334, Moscow, Russia.
³ Institute of Gene Biology, Russian Academy of Sciences, Vavilova str., 34/5, 119334, Moscow, Russia.
⁴ Apto-Pharm Ltd, Kolomensky dr., 13A, 115564, Moscow, Russia; Sechenov First Moscow State Medical University, Institute of Molecular Medicine, Trubetskaya str. 8-2, 119048, Moscow, Russia.

PMID: 31813549
DOI: 10.1016/j.bbrc.2019.11.190

Abstract

Oligonucleotide RA36 contains two G-quadruplex modules with thrombin binding aptamer sequence GGTTGGTGTGGTTGG. Each of the modules potentially can bind thrombin while differing in functional activity. Despite that, previously published studies report a single dissociation constant for the thrombin:RA36 complex, which value varies widely. Here we address this discrepancy using electrophoretic mobility shift assay. Our results reveal that the interaction between RA36 and thrombin is a two-stage process. The two modules have different affinities for thrombin, which explains the discrepancy in the published data.

Keywords: Dissociation constant; Electrophoretic mobility shift assay; Oligonucleotide; RA36; Thrombin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Electrophoretic Mobility Shift Assay
Humans
Oligonucleotides / metabolism*
Protein Binding
Thrombin / metabolism*

Substances

Oligonucleotides
Thrombin