Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0031196
Title: Probing high affinity sequences of DNA aptamer against VEGF 165
Authors: Kaur, H.
Yung, L.-Y.L. 
Issue Date: 16-Feb-2012
Source: Kaur, H., Yung, L.-Y.L. (2012-02-16). Probing high affinity sequences of DNA aptamer against VEGF 165. PLoS ONE 7 (2) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0031196
Abstract: Vascular endothelial growth factor (VEGF 165) is a potent angiogenic mitogen commonly overexpressed in cancerous cells. It contains two main binding domains, the receptor-binding domain (RBD) and the heparin-binding domain (HBD). This study attempted to identify the specific sequences of the VEa5 DNA aptamer that exhibit high binding affinity towards the VEGF 165 protein by truncating the original VEa5 aptamer into different segments. Using surface plasmon resonance (SPR) spectroscopy for binding affinity analysis, one of the truncated aptamers showed a >200-fold increase in the binding affinity for HBD. This truncated aptamer also exhibited high specificity to HBD with negligible binding affinity for VEGF 121, an isoform of VEGF lacking HBD. Exposing colorectal cancer cells to the truncated aptamer sequence further confirmed the binding affinity and specificity of the aptamer to the target VEGF 165 protein. Hence, our approach of aptamer truncation can potentially be useful in identifying high affinity aptamer sequences for the biological molecules and targeting them as antagonist for cancer cell detection. © 2012 Kaur, Yung.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/89938
ISSN: 19326203
DOI: 10.1371/journal.pone.0031196
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

39
checked on Feb 14, 2018

WEB OF SCIENCETM
Citations

35
checked on Jan 16, 2018

Page view(s)

41
checked on Feb 18, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.