Saccharin inhibits carbonic anhydrases:: Possible explanation for its unpleasant metallic aftertaste

被引：154

作者：

Koehler, Karen

Hillebrecht, Alexander

Wischeler, Johannes Schulze

Innocenti, Alessio

Heine, Andreas

Supuran, Claudiu T.

Klebe, Gerhard

机构：

[1] Univ Marburg, Inst Pharmaceut Chem, D-35032 Marburg, Germany

[2] Univ Florence, Dipartimento Chim, Lab Chim Bioinorgan, I-50019 Sesto Fiorentino, Italy

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 40期

关键词：

carbonic anhydrase; homology models; isoforms; saccharin; structure elucidation;

D O I：

10.1002/anie.200701189

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A matter of taste: The sweetner saccharin (a cyclic sulfimide, see picture) is nearly completely absorbed and eliminated through the urine, and is thus exposed to many different proteins in the body. It binds at nanomolar levels to some carbonic anhydrases and this provokes the question of its inert properties. It is known that the plasma level slowly decreases after oral dosing, and CAVI binding could explain its unpleasant metallic aftertaste. (Figure Presented). © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：7697 / 7699

页数：3

共 13 条

[1] Nonaromatic sulfonamide group as an ideal anchor for potent human carbonic anhydrase inhibitors: Role of hydrogen-bonding networks in ligand binding and drug design [J].