神经激肽A和B的羧基末端七肽片段二聚化增强了对速激肽受体亚型的选择性。

Dimerization of neurokinin A and B COOH-terminal heptapeptide fragments enhanced the selectivity for tachykinin receptor subtypes.

作者信息

Kodama H, Shimohigashi Y, Sakaguchi K, Waki M, Takano Y, Yamada A, Hatae Y, Kamiya H

机构信息

Laboratory of Biochemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.

出版信息

Eur J Pharmacol. 1988 Jul 7;151(2):317-20. doi: 10.1016/0014-2999(88)90815-1.

DOI:10.1016/0014-2999(88)90815-1

PMID:2844557

Abstract

We have synthesized dimeric analogues of neurokinin A and B COOH-terminal heptapeptide fragments and evaluated their biological activities to contract isolated smooth muscle preparations of the guinea-pig ileum and rat vas deferens. The dimers were fairly active and showed two-fold increased selectivity for receptors in the guinea-pig ileum as compared with monomers. Extremely slow dissociation indicated a possible bivalent interaction between dimer and receptor.

摘要

我们合成了神经激肽A和B的羧基末端七肽片段的二聚体类似物，并评估了它们对豚鼠回肠和大鼠输精管的离体平滑肌制剂产生收缩作用的生物活性。这些二聚体相当活跃，与单体相比，对豚鼠回肠中的受体具有两倍的选择性增加。极慢的解离表明二聚体与受体之间可能存在二价相互作用。