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    National Tsing Hua University Institutional Repository > 原子科學院  > 生醫工程與環境科學系 > 期刊論文 >  Determining the binding mode and binding affinity constant of tyrosine kinase inhibitor PD153035 to DNA using optical tweezers


    Please use this identifier to cite or link to this item: http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/61802


    Title: Determining the binding mode and binding affinity constant of tyrosine kinase inhibitor PD153035 to DNA using optical tweezers
    Authors: Cheng CM;Lee YJ;Wang WT;Hsu CT;Tsai JS;Wu CM;Ou KL;Yang TS
    教師: 吳見明
    Date: 2011
    Publisher: ELSEVIER
    Relation: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Volume: 404, Issue: 1, Pages: 297-301
    Keywords: PD153035
    Non-small cell lung cancer
    Tyrosine kinase inhibitor
    Binding affinity constant
    Optical tweezers
    Wormlike chain model
    Abstract: Accurately predicting binding affinity constant (K-A) is highly required to determine the binding energetics of the driving forces in drug-DNA interactions. Recently, PD153035, brominated anilinoquinazoline, has been reported to be not only a highly selective inhibitor of epidermal growth factor receptor but also a DNA intercalator. Here, we use a dual-trap optical tweezers to determining K-A for PD153035, where K-A is determined from the changes in B-form contour length (L) of PD153035-DNA complex. Here, L is fitted using a modified wormlike chain model. We found that a noticeable increment in L in 1 mM sodium cacodylate was exhibited. Furthermore, our results showed that K-A = 1.18(+/-0.09) x 10(4) (1/M) at 23 +/- 0.5 degrees C and the minimum distance between adjacent bound PD153035 approximate to 11 bp. We anticipate that by using this approach we can determine the complete thermodynamic profiles due to the presence of DNA intercalators.
    URI: http://www.elsevier.com/
    http://nthur.lib.nthu.edu.tw/dspace/handle/987654321/61802
    Appears in Collections:[生醫工程與環境科學系] 期刊論文

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