Role of the galactosyl moiety of collagen glycopeptides for T-cell stimulation in a model for rheumatoid arthritis
Research output: Contribution to journal › Article
Abstract
Two protected derivatives of beta-D-galactopyranosyl-5-hydroxy-L-lysine, in which HO-4 of galactose has been O-methylated or replaced by fluorine, have been prepared. The building blocks were incorporated at position 264 of the peptide fragment CII259-273 from type II collagen by solid-phase synthesis. The ability of these two glycopeptides, and two CII259-273 glycopeptides in which HO-4 of galactose was either unmodified or deoxygenated, to elicit responses from T-cell hybridomas obtained in a mouse model for rheumatoid arthritis was then determined. The hybridomas were all highly sensitive towards modifications at C-4 of the beta-D-galactosyl residue of CII259-273, highlighting the role of HO-4 as an important contact point for the T-cell receptor. Most likely, this glycopeptide hydroxyl group is involved in hydrogen bonding with the T-cell receptor. (C) 2003 Elsevier Ltd. All rights reserved.
Details
Authors | |
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Organisations | |
Research areas and keywords | Subject classification (UKÄ) – MANDATORY
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Original language | English |
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Pages (from-to) | 3981-3987 |
Journal | Bioorganic & Medicinal Chemistry |
Volume | 11 |
Issue number | 18 |
Publication status | Published - 2003 |
Publication category | Research |
Peer-reviewed | Yes |
Bibliographic note
The information about affiliations in this record was updated in December 2015.
The record was previously connected to the following departments: Medical Inflammation Research (013212019)