Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0050964
Title: Investigating the Antiproliferative Activity of High Affinity DNA Aptamer on Cancer Cells
Authors: Kaur, H.
Li, J.J.
Bay, B.-H.
Yung, L.-Y.L. 
Issue Date: 16-Jan-2013
Source: Kaur, H., Li, J.J., Bay, B.-H., Yung, L.-Y.L. (2013-01-16). Investigating the Antiproliferative Activity of High Affinity DNA Aptamer on Cancer Cells. PLoS ONE 8 (1) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0050964
Abstract: Vascular endothelial growth factor (VEGF) is an angiogenic mitogen involved in promoting tumor angiogenesis inside the body. VEGF is a key protein required for progression of tumor from benign to malignant phenotype. In this study, we investigated the binding affinity of a previously selected 26-mer DNA aptamer sequence (SL2-B) against heparin binding domain (HBD) of VEGF165 protein. The SL2-B was first chemically modified by introduction of phosphorothioate linkages (PS-linkages). Subsequently, surface plasmon resonance (SPR) spectroscopy and circular dichroism (CD) were used to determine the binding affinity, specificity and to deduce the conformation of PS-modified SL2-B sequence. Finally, antiproliferative activity of the modified SL2-B sequence on Hep G2 cancer cells was investigated. Our results demonstrate a marked enhancement in the biostability of the SL2-B sequence after PS modification. The modified SL2-B sequence also exhibits enhanced antiproliferative activity against Hep G2 cancer cells in hypoxia conditions. In addition, modified SL2-B sequence inhibits the expression of Jagged-1 protein, which is one of the ligands to VEGF linked delta/jagged-notch signaling pathway. © 2013 Kaur et al.
Source Title: PLoS ONE
URI: http://scholarbank.nus.edu.sg/handle/10635/89279
ISSN: 19326203
DOI: 10.1371/journal.pone.0050964
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