Synthesis of a molecular mimic of the Glc1Man9 oligoside as potential inhibitor of calnexin binding to ΔF508 CFTR protein

被引：5

作者：

Cherif, S

Leach, MR

Williams, DB

Monneret, C

机构：

[1] CNRS, UMR 176, Inst Curie, Sect Rech, F-75248 Paris 05, France

[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 2002年 / 12卷 / 09期

关键词：

D O I：

10.1016/S0960-894X(02)00151-8

中图分类号：

R914 [药物化学];

学科分类号：

100701 [药物化学];

摘要：

Deletion of phenylalanine at position 508 of the CFTR protein is associated with a severe form of cystic fibrosis. Biosynthetic arrest of the misfolded DeltaF508 CFTR protein in the endoplasmic reticulum is due to prolonged interaction with protein chaperones. In order to overcome this retention and thereby restore the delivery of the protein to the plasma membrane, a molecular mimic of the glycoprotein oligoside moiety has been designed and synthesized. Ability of this mimic to inhibit the binding of the natural Glc(1)Man(9)GIcNAc oligoside to calnexin has been measured. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：1237 / 1240

页数：4

共 19 条

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TETRAFLUOROBORIC ACID, AN EFFICIENT CATALYST IN CARBOHYDRATE PROTECTION AND DEPROTECTION REACTIONS [J].