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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/25133


    Title: Preferential binding to DNA sequences of peptides related to a novel XPRK motif
    Authors: 鄭建中;Cheng, Chien-chung;Yang, Chia-hung;Chou, Ping-jen;Luo, Zhen-long;Chou, I. Chun;Chang, Jung-cheng;Cheng, Chien-chung;Christopher R. H.;Martin, Michael. J. Waring,;Leung Sheh
    Contributors: 淡江大學化學學系
    Date: 2003-07-31
    Issue Date: 2009-12-01
    Publisher: Elsevier
    Abstract: Two dodecapeptide amines: (WPRK)(3)NH(2)[WR-12] and (YPRK)(3)NH(2)[YR-12], and a 30-mer polypeptide amide (SP-30) were synthesized by solid-phase peptide methodology. DNase I footprinting studies on a 117-mer DNA showed that WR-12 and YR-12 bind selectively to DNA sequences in a manner similar to SP-30 which has a repeating SPK(R)K sequence. The most distinctive blockages seen with all three peptides occur at positions 26-30, 21-24 and 38-45 around sequences 5'-GAATT-3', 5'-TAAT-3' and 5'-AAAACGAC-3', respectively. However, it appears that YR-12 is better able to extend its recognition site to include CG pairs than is SP-30. At low concentrations YR-12 was able to induce enhanced rates of DNase I cleavage at regions surrounding some of its binding sites. To obtain further quantitative data supplementary to the footprinting work, equilibrium binding experiments were performed in which the binding of the two peptides to six decanucleotide duplexes was compared. Scatchard analyses indicated that WR-12 may be more selective for oligomers containing runs of consecutive purines or pyrimidines. On the other hand, YR-12 binds better to d(CTTAGACGTC)- d(GACGTCTAAG) than to the other oligomer duplexes, denoting selectivity for evenly distributed C/G and A/T sequences.
    Relation: Bioorganic and medicinal chemistry 11(15), pp.3279-3288
    DOI: 10.1016/S0968-0896(03)00279-7
    Appears in Collections:[化學學系暨研究所] 期刊論文

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