Hydrophilic photolabelling of glycopeptides from the murine liver-intestine (LI) cadherin recognition domain

被引：15
|
作者：
Heiner, Sebastian [1 ]
Detert, Heiner [1 ]
Kuhn, Axel [1 ]
Kunz, Horst [1 ]
机构：
[1] Univ Mainz, Inst Organ Chem, D-55099 Mainz, Germany
来源：
BIOORGANIC & MEDICINAL CHEMISTRY | 2006年 / 14卷 / 18期
关键词：
glycopeptides; LI-cadherin; coumarine chromophore; sialyl-T antigen; solid-phase synthesis;
D O I：
10.1016/j.bmc.2006.06.014
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：
LI-Cadherin is a transmembrane glycoprotein involved in cell adhesion of epithelial cells. Its supposed recognition domain contains the peptide motif AAL and is distinctly hydrophobic. In order to obtain sufficiently soluble model compounds, glycan side chains of T-antigen, (2,6)sialyl T-antigen and sialyl T-N-antigen structure were linked to the serine located in the supposed turn sequence of the LI-cadherin recognition domain. A quinic acid-glycine-7-amino-coumarine (Quiglac) chromophore was constructed in order to enhance the solubility of labelled LI-cadherin (glyco)peptides in water. (c) 2006 Elsevier Ltd. All rights reserved.
引用
收藏
页码：6149 / 6164
页数：16
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