Okada Y, Tsuboi S, Tsuda Y, Nagamatsu Y, Yamamoto J
Faculty of Pharmaceutical Sciences, Kobe-Gakuin University, Japan.
FEBS Lett. 1990 Oct 15;272(1-2):113-6. doi: 10.1016/0014-5793(90)80461-q.
A trihexacontapeptide corresponding to the sequence 8-70 of eglin c and its related peptides were synthesized by the conventional solution method and their inhibitory activity against human leukocyte elastase, cathepsin G and alpha-chymotrypsin was examined. Although synthetic eglin c (41-49) inhibited cathepsin G and alpha-chymotrypsin (Ki = 4.0 x 10(-5) M and 2.0 x 10(-5) M, respectively) but not leukocyte elastase, the synthetic trihexacontapeptide potently inhibited cathepsin G, alpha-chymotrypsin and leukocyte elastase (Ki = 1.8 x 10(-9) M, 1.4 x 10(-9) M and 2.2 x 10(-9) M, respectively). The relationship between the structure of eglin c and the inhibitory activity against the above enzymes is also described.
通过传统溶液法合成了对应于水蛭素c序列8 - 70的三十六肽及其相关肽，并检测了它们对人白细胞弹性蛋白酶、组织蛋白酶G和α-胰凝乳蛋白酶的抑制活性。虽然合成的水蛭素c（41 - 49）抑制组织蛋白酶G和α-胰凝乳蛋白酶（Ki分别为4.0×10⁻⁵ M和2.0×10⁻⁵ M），但不抑制白细胞弹性蛋白酶，而合成的三十六肽则能有效抑制组织蛋白酶G、α-胰凝乳蛋白酶和白细胞弹性蛋白酶（Ki分别为1.8×10⁻⁹ M、1.4×10⁻⁹ M和2.2×10⁻⁹ M）。还描述了水蛭素c的结构与对上述酶的抑制活性之间的关系。
