高等学校化学学报 ›› 2000, Vol. 21 ›› Issue (2): 241.

• 论文 • 上一篇    下一篇

多肽与花粉钙调素的相互作用及对细胞功能的影响

苏静1, 宋艳玲1, 阎虎生2   

  1. 1. 北京大学化学与分子工程学院, 北京 100871;
    2. 南开大学高分子化学研究所, 天津 300071
  • 收稿日期:1999-07-09 出版日期:2000-02-24 发布日期:2000-02-24
  • 通讯作者: 宋艳玲(1941年出生),女,副教授,主要从事活性肽的合成与应用研究.
  • 基金资助:

    国家自然科学基金(批准号:29672002)资助

Interaction of Peptides with Pollen Camodulin and Their Effects on Cellular Functions

SU Jing1, SONG Yan-Ling1, YAN Hu-Sheng2   

  1. 1. College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China;
    2. Institute of Polymer Chemistry, Nankai University, Tianjin 300071, China
  • Received:1999-07-09 Online:2000-02-24 Published:2000-02-24

摘要: 研究了在Ca2+存在下,丹磺酰标记的花粉钙调素(D-pCaM)与合成的多肽相互作用的规律.研究结果表明,被研究的绝大多数多肽能与D-pCaM结合而形成复合物,使D-pCaM的荧光光谱发生变化.用荧光法测定了这些复合物的解离常数Kd,其中肽BP-13的Kd值为4.0nmol/L,是与pCaM结合能力最强的一个多肽.除证明了多肽的疏水性,预测二级结构形成倾向和链长对其与pCaM结合能力有影响外,还发现用D-丙氨酸取代肽链中的Gly或L-丙氨酸后,可改变肽对pCaM的亲和性,这为提高多肽与钙调素的亲和力提供了一条改进的途径.我们的研究还可以定性地说明不同来源CaM性质相似又有差异,反映了它们的高度保守性和变异性.同时还展示了所研究的多肽对细胞信息传导过程的影响,为研究CaM对细胞功能调节的作用机制和建立pCaM拮抗肽的活性筛选模型提供了思路.

关键词: 花粉钙调素, 细胞信息传导, 亲合性, 多肽

Abstract: The interaction between dansyl-labeled pollen calmodulin(D-pCaM) and buckwheat pollen peptide analogs was studied in the presence of Ca2+. Most peptides in our research can associate with D-pCaMand form peptide-pCaMcomplexes, which changed the fluorescence spectra of D-pCaM. The dissociation constants Kdfor these complexes were determined using fluorescence titration. Peptide BP-13, AMALALKKTGNH2, had the smallest Kdvalue 4.0 nmol/L, demonstrating the highest affinity for pCaM. In addition to studying the influence of hydrophobicity, propensity of secondary structure and chain length on these peptides abilities to bind pCaM, we have also found that Gly/L-Ala→D-Ala substitution in peptide chains caused great changes in their affinity for pCaM. These results suggest a potentially useful approach to improving the binding ability of peptidic antagonist to CaM. Furthermore, our data provided evidence on the dissimilarity of different CaMs although they have highly-conserved structures. Aprimary study was carried out on the effects of CaM-binding peptides on cellular signal transduction, cell proliferation and growth, showing the participation of CaMin this important cellular life process.

Key words: Pollen calmodulin, Cellular signal transduction, Affinity, Peptide

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