摘要
研究了在Ｃａ２＋ 存在下荞麦花粉肽及其类似物和丹磺酰标记的钙调素（Ｄ－ＣａＭ）的相互作用， 结果表明， 除肽ＢＰ－１ 外， 都能与Ｄ－ＣａＭ 结合而形成复合物． 利用荧光光谱法测定了这些复合物的解离常数Ｋｄ． 在所研究的多肽中以ＢＰ－１３ 拮抗ＣａＭ 作用最强， 其Ｋｄ 值为４．６×１０－ ２μｍ ｏｌ／Ｌ， 抑制钙依赖性磷酸二酯酶活性的ＩＣ５０为２．２ μｍ ｏｌ／Ｌ． 我们还发现， 当Ｄ－丙氨酸残基取代没有亲和性的ＢＰ－１ 中甘氨酸残基时， 其亲和性明显提高．
The interactions of the buckwheat pollen peptide and its analogues with dansyl labeled calmodulin( D CaM) were studied in the presence of Ca 2+ . All peptides except BP 1 can associate with D CaM to form complexes peptide calmodulin. The dissociation constants K d for the complexes were determined using the fluorescence spectra. Among the tested peptides, BP 13 showed a stronger inhibitory effect on CaM, with IC 50 of 2.2 μmol/L and K d of 4.6×10 -2 μmol/L. The effects of the hydrophobicity and the behavior being predicated to have a higher α helical propensities on their affinities were further studied. We have found that D alanine substitution in BP 1 results in affinity enhancement. The result will be helpful to improving our ability to design peptides possessing anticalmodulin activity.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
1999年第11期1738-1742,共5页
Chemical Journal of Chinese Universities
基金
国家自然科学基金
关键词
钙调素拮抗剂
花粉多肽
拮抗剂
Pollen peptide, Calmodulin, Calmodulin antagonist
