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Binding and Structural Properties of DNA Aptamers with VEGF-A-Mimic Activity

Toru Yoshitomi, Misako Hayashi, Takumi Oguro, Keiko Kimura, Fumiya Wayama, Hitoshi Furusho, Sciprofile linkKeitaro Yoshimoto
Published: 1 March 2020
Molecular Therapy - Nucleic Acids , Volume 19, pp 1145-1152; doi:10.1016/j.omtn.2019.12.034

Abstract: Vascular endothelial growth factors (VEGFs) are hypoxia-inducible secreted proteins to promote angiogenesis, in which VEGF-A is an important molecule that binds and activates VEGF receptor-1 (VEGFR-1) and VEGFR-2. In this study, two DNA aptamers, Apt01 and Apt02, were successfully isolated by alternating consecutive systematic evolution of ligands by exponential enrichment (SELEX) against VEGFR-1 and -2 using deep sequencing analysis in an early selection round. Their binding affinities for VEGFR-2 were lower than that of VEGFR-1, which is similar to that of VEGF-A. Structural analyses with the measurements of circular dichroism spectra and ultraviolet melting curve showed that Apt01 possessed the stem-loop structure in the molecule, whereas Apt02 formed G-quadruplex structures. In addition, Apt02 accelerated a tube formation of human umbilical vein endothelial cells faster than Apt01, which was affected by difference of binding affinity and nuclease resistance due to G-quadruplex structures. These results demonstrated that Apt02 might have a potential to function as an alternative to VEGF-A.
Keywords: angiogenesis / vascular endothelial growth factor / Vegf / G-Quadruplex / aptamer / Vegf Receptor

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