Sp1蛋白锌指结构域及其模拟物的合成及与寡聚核苷酸结合能力的研究

用固相多肽合成方法首次合成转录因子Sp1的第2个锌指Sp1-ZF2及其突变体Sp1-ZF2/HT(E²⁰→H,R²³→T),模拟物ZF20和ZF15.CD谱及Co(Ⅱ)UV-可见光谱研究表明:当缺少足够的疏水氨基酸以及Cys与His距离改变时,锌指结构的形成将受到影响.凝胶阻滞电泳研究表明:突变的两位置显著影响特异识别.单个锌指肽可以与特异性寡聚核苷酸序列结合.     

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

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.