Investigation of the interaction between split aptamer and vascular endothelial growth factor 165 using single molecule force spectroscopy. Issue 5 (9th December 2019)

• Record Type: Journal Article
• Authors: Li, Shaoyuan; Zheng, Yan; Liu, Yaqin; Geng, Xiuhua; Liu, Xiaofeng; Zou, Liyuan; Wang, Qing; Yang, Xiaohai; Wang, Kemin
• Is Part Of: Journal of molecular recognition. Volume 33:Issue 5(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2019-12-09
• Subjects: dynamic force spectroscopy -- interaction -- single molecule force spectroscopy -- split aptamer -- vascular endothelial growth factor 165; Molecular recognition -- Periodicals; Models, Molecular -- Periodicals; Molecular Conformation -- Periodicals; Molecular Sequence Data -- Periodicals; Molecular Structure -- Periodicals; Carrier Proteins -- Periodicals; 572.8
• DOI: 10.1002/jmr.2829
• Languages: English
• ISSNs: 0952-3499

Abstract

Abstract: 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/VEGF165 was 169.44 ± 6.59 pN at the loading rate of 35.2 nN/s, and the binding probability of split aptamer/VEGF165 was dependent on the concentration of VEGF165 . On the basis of dynamic force spectroscopy results, one activation barrier in the dissociation process of split aptamer/VEGF165 complexes was revealed, which was similar to that of the intact aptamer/VEGF165 . Besides, the dissociation rate constant ( k off ) of split aptamer/VEGF165 was close to that of intact aptamer/VEGF165, and the interaction force of split aptamer/VEGF165 was higher than the force of intact aptamer/VEGF165 . It indicated that split aptamer also possessed high affinity with VEGF165 . The work can provide a new method for exploring the interaction of split aptamer/its targets at single‐molecule level. Abstract : The interactions between split aptamer and vascular endothelial growth factor 165 (VEGF165 ) was investigated by single molecule force spectroscopy. The similar dissociation path in the dissociation process between split aptamer/VEGF165 and intact aptamer/VEGF165 were observed, indicating that split aptamer still possessed high affinity with VEGF165 .