Synthesis and DNA-binding ability of Spl protein zinc finger domain and its peptidomimetics  

作　　者：王锐 倪京满 胡晓愚 马亚平 李向群 杨顶建 董守良 杨晓武 潘鑫复 

机构地区：[1]Department of Biology, State Key Laboratory of Applied Organic Chemistry, Lanzhou University, Lanzhou 730000, China

出　　处：《Science China(Life Sciences)》1997年第5期518-523,共6页中国科学（生命科学英文版）

基　　金：Project supported by the Fok Ying Tung Education Foundation, the National Natural Science Foundation of China, and the State Education Commission of China.

摘　　要：The second zinc finger fragment of Sp1 (Spl-ZF2), its mutant (Spl-ZF2/HT. E20→H, R23→T), and two mimic analogues (ZF20 and ZF15) were synthesized by stepwise solid phase technique. The CD spectra and UV-visible spectrum with CoCl2 indicated that the formation of zinc finger structure was affected not only by the hy-drophobic amino acids but also by the change of the distance between Cys and His. Gel-retardation electrophoresis as-says indicated that the Grlu and Arg residues are very important for recognition. A single zinc finger like Spl-ZF2 isable to bind DNA sequence specifically.The second zinc finger fragment of Sp1 (Spl-ZF2), its mutant (Spl-ZF2/HT. E20→H, R23→T), and two mimic analogues (ZF20 and ZF15) were synthesized by stepwise solid phase technique. The CD spectra and UV-visible spectrum with CoCl2 indicated that the formation of zinc finger structure was affected not only by the hy-drophobic amino acids but also by the change of the distance between Cys and His. Gel-retardation electrophoresis as-says indicated that the Grlu and Arg residues are very important for recognition. A single zinc finger like Spl-ZF2 isable to bind DNA sequence specifically.

关 键 词：zinc FINGER domain SP1 protein solid phase peptide SYNTHESIS sequence specifically oligonucleotide. 

分 类 号：Q52[生物学—生物化学]