Investigating a quadruplex-ligand interaction by unfolding kinetics

被引:30
作者
Green, Jeremy J. [1 ]
Ladame, Sylvain [1 ]
Ying, Liming [1 ]
Klenerman, David [1 ]
Balasubramanian, Shankar [1 ]
机构
[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England
关键词
D O I
10.1021/ja0615425
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
We have investigated the interaction of the intramolecular human telomeric DNA G-quadruplex with a hemicyanine-peptide ligand, by studying the rate of quadruplex opening with a complementary DNA oligonucleotide. By employing a minimal kinetic model, the relationship between the observed rate of quadruplex opening and the ligand concentration has enabled estimation of the dissociation constant. A van't Hoff analysis revealed the enthalpy and entropy changes of binding to be -77 +/- 22 kJ mol(-1) and -163 +/- 75 J mol(-1) K-1, respectively. Arrhenius analyses of the rate constants of opening free and bound quadruplex gave activation energies of 118 +/- 2 and 98 +/- 10 kJ mol(-1), respectively. These results indicate that the presence of the ligand has only a small effect on the activation energy, suggesting that the unbinding of the ligand occurs after the transition state for quadruplex unfolding.
引用
收藏
页码:9809 / 9812
页数:4
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