摘要
本文设计并采用固相法合成了4种钙调蛋白可结合多肽,这些多肽分成两组,每一组中两个多肽的碱性和疏水性相近,但形成α螺旋结构的倾向(预测)不同。研究了这些多肽与钙调蛋白的相互作用,在Ca^(2+)存在下,这些多肽与丹磺酰钙调蛋白结合,使丹磺酰钙调蛋白的荧光光谱发生显著变化,测定了多肽与钙调蛋白所形成的复合物的解离常数。结果表明,预测形成α螺旋结构倾向较大的多肽与钙调蛋白的亲合力也较大。
Four calmodulin-binding peptides were designed and synthesized by the solid-phase method. They are separated into two groups. In each group the two peptides have similar basicities and hydrophobicities,but they have different propensities to form α-helices (predicted) .The interactions of the peptides with calmodulin were studied. In the presence of Ca2+, the peptides associate with dansyl calmodulin. The fluorescence spectra of dansyl calmodulin change dramtically on the binding of the peptides. The dissociation constants for the complexes of the peptides with calmodulin were determined. The results indicate that the peptides which were predicted to have higher α-helical propensities have higher affinities to calmodulin.
出处
《生物化学杂志》
CAS
CSCD
1991年第2期147-152,共6页
关键词
多肽
α螺旋结构
钙调蛋白
Calmodulin
Peptide
Solid-phase synthesis
α-Helix
