Title of article
Hydrophilic photolabelling of glycopeptides from the murine liver–intestine (LI) cadherin recognition domain Original Research Article
Author/Authors
Sebastian Heiner، نويسنده , , Heiner Detert، نويسنده , , Axel Kuhn، نويسنده , , Horst Kunz، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2006
Pages
16
From page
6149
To page
6164
Abstract
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 TN-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.
Keywords
Coumarine chromophore , LI-cadherin , Solid-phase synthesis , Glycopeptides , Sialyl-T antigen
Journal title
Bioorganic and Medicinal Chemistry
Serial Year
2006
Journal title
Bioorganic and Medicinal Chemistry
Record number
1304618
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