Regulation of thrombin activity by ligand-induced topological alteration in a thrombin-binding aptamer

Thrombin-binding aptamer (TBA), which forms a G-quadruplex (G4) structure with anti-parallel topology, interacts with thrombin to inhibit its enzymatic activity. Here we show that the G4-topology-altering ligand L2H2-2M2EA- 6LCO ( 6LCO ) changes the anti-parallel topology of TBA G4 to the parallel t...

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Published inChemical communications (Cambridge, England) Vol. 59; no. 57; pp. 8862 - 8865
Main Authors Sasaki, Shogo, Ma, Yue, Hirokawa, Takatsugu, Ikebukuro, Kazunori, Tera, Masayuki, Nagasawa, Kazuo
Format Journal Article
LanguageEnglish
Published England Royal Society of Chemistry 13.07.2023
Subjects
Binding
Ligands
Thrombin
Topology
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Summary:Thrombin-binding aptamer (TBA), which forms a G-quadruplex (G4) structure with anti-parallel topology, interacts with thrombin to inhibit its enzymatic activity. Here we show that the G4-topology-altering ligand L2H2-2M2EA- 6LCO ( 6LCO ) changes the anti-parallel topology of TBA G4 to the parallel topology, thereby abrogating the thrombin-inhibitory activity of TBA. This finding suggests that G4 ligands that alter topology may be promising drug candidates for diseases involving G4-binding proteins. The function of the thrombin-binding aptamer was regulated by the G-quadruplex topology-altering ligand of L2H2-2M2EA- 6LCO , thereby controlling thrombin activity.
Bibliography:https://doi.org/10.1039/d3cc02308g
Electronic supplementary information (ESI) available. See DOI
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ISSN:1359-7345
1364-548X
1364-548X
DOI:10.1039/d3cc02308g