A Jemal

AD Ellington

AM Kawasaki

Antonio Facchiano

B Barleon

B Millauer

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BA Keyt

BE Eaton

Boon-Huat Bay

C Tuerk

CJ Robinson

DJ Price

F Fan

F Radtke

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H Suzuki

Harleen Kaur

J Baselga

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J Gao

J Itakura

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J Oswald

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J Waltenberger

Jasmine J. Li

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Lin-Yue Lanry Yung

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PE Burmeister

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SF Wong

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X Jiang

Y Lin

Z Wang

PLoS ONE

PubMed

Kaur Harleen

Li Jasmine J.

Bay Boon-Huat

Yung Lin-Yue Lanry

Public Library of Science (PLOS)

Investigating the Antiproliferative Activity of High Affinity DNA Aptamer on Cancer Cells

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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 (SL(2)-B) against heparin binding domain (HBD) of VEGF(165) protein. The SL(2)-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 SL(2)-B sequence. Finally, antiproliferative activity of the modified SL(2)-B sequence on Hep G2 cancer cells was investigated. Our results demonstrate a marked enhancement in the biostability of the SL(2)-B sequence after PS modification. The modified SL(2)-B sequence also exhibits enhanced antiproliferative activity against Hep G2 cancer cells in hypoxia conditions. In addition, modified SL(2)-B sequence inhibits the expression of Jagged-1 protein, which is one of the ligands to VEGF linked delta/jagged-notch signaling pathway

Jasmine J Li

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Investigating the antiproliferative activity of high affinity DNA aptamer on cancer cells.

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Investigating the Antiproliferative Activity of High Affinity DNA Aptamer on Cancer Cells

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Directory of Open Access Journals

Public Library of Science (PLOS)