Development of inhibitors based on short helical peptides for protein-protein interactions

我探索了α-螺旋稳定对短肽与dna结合的影响。用靶DNA双链滴定基于转录因子同源结构域的交联肽时，计算出其解离常数（Kd）约为0.5 nM。该值比相应的非交联肽小两位数。该交联肽显示出与原始dna结合蛋白相同水平的高底物特异性。

I explored the effect of α-helical stabilization upon the binding of short peptides to DNAs. When a cross-linked peptide based on the homeodomain of transcription factor was titrated with a target DNA duplex, its dissociation constant (Kd) was calculated to be ca. 0.5 nM. This value was the double-digit smaller than that of the corresponding non-cross-linked peptide. The cross-linked peptide showed high substrate specificity for DNAs at the same level as the original DNA-binding protein.