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Investigation of the interaction between split aptamer and vascular endothelial growth factor 165 using single molecule force spectroscopy
Author(s) -
Li Shaoyuan,
Zheng Yan,
Liu Yaqin,
Geng Xiuhua,
Liu Xiaofeng,
Zou Liyuan,
Wang Qing,
Yang Xiaohai,
Wang Kemin
Publication year - 2020
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.2829
Subject(s) - aptamer , force spectroscopy , vegf receptors , dissociation constant , biophysics , chemistry , vascular endothelial growth factor , dissociation (chemistry) , molecule , biology , microbiology and biotechnology , biochemistry , receptor , cancer research , organic chemistry
Understanding the binding of split aptamer/its target could become a breakthrough in the application of split aptamer. Herein, vascular endothelial growth factor (VEGF), a major biomarker of human diseases, was used as a model, and its interaction with split aptamer was explored with single molecule force spectroscopy (SMFS). SMFS demonstrated that the interaction force of split aptamer/VEGF 165 was 169.44 ± 6.59 pN at the loading rate of 35.2 nN/s, and the binding probability of split aptamer/VEGF 165 was dependent on the concentration of VEGF 165 . On the basis of dynamic force spectroscopy results, one activation barrier in the dissociation process of split aptamer/VEGF 165 complexes was revealed, which was similar to that of the intact aptamer/VEGF 165 . Besides, the dissociation rate constant ( k off ) of split aptamer/VEGF 165 was close to that of intact aptamer/VEGF 165 , and the interaction force of split aptamer/VEGF 165 was higher than the force of intact aptamer/VEGF 165 . It indicated that split aptamer also possessed high affinity with VEGF 165 . The work can provide a new method for exploring the interaction of split aptamer/its targets at single‐molecule level.