Binding of tryptamine analogs at h5-HT1E receptors:: a structure-affinity investigation

被引：18

作者：

Dukat, M

Smith, C

Herrick-Davis, K

Teitler, M

Glennon, RA

机构：

[1] Virginia Commonwealth Univ, Sch Pharm, Dept Med Chem, Richmond, VA 23298 USA

[2] Albany Med Coll, Dept Pharmacol & Neurosci, Albany, NY 12208 USA

来源：

BIOORGANIC & MEDICINAL CHEMISTRY | 2004年 / 12卷 / 10期

关键词：

serotonin receptors; ergolines;

D O I：

10.1016/j.bmc.2004.03.026

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structure-affinity requirements for the binding of serotonin (5-HT) analogs at human 5-HT1E receptors were investigated by examining the affinities of >40 tryptamine-related compounds. No tryptamine analog was found to bind with substantially higher affinity than 5-HT. The results indicate that hydrogen bonding plays a key role in the 5-HT1E/receptor interaction. This finding was supported using quantitative structure-activity analysis (QSAR) techniques such as comparative molecular field analysis (CoMFA) and the program QsarIS. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：2545 / 2552

页数：8

共 26 条

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