Synthesis of lipopeptides of the immunodominant epitope hMBP(83–99) containing amide or C-C bond linked hydrophobic chains for the study of T cell response
Autor: | G. Rapi, Luca Massacesi, Marco Vergelli, Mario Chelli, Elena Nardi, Anna Maria Papini, Luigi Amaducci, Benedetta Mazzanti, Silvia Mazzucco, Mauro Ginanneschi |
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Rok vydání: | 1999 |
Předmět: |
chemistry.chemical_classification
biology Stereochemistry T cell Diastereomer Lipopeptide Bioengineering Peptide Biochemistry In vitro Epitope Analytical Chemistry Myelin basic protein chemistry.chemical_compound medicine.anatomical_structure chemistry Amide Drug Discovery biology.protein medicine Molecular Medicine |
Zdroj: | Letters in Peptide Science. 6:51-59 |
ISSN: | 1573-3904 0929-5666 |
DOI: | 10.1007/bf02443618 |
Popis: | We previously demonstrated that the lipopeptide of the myelin basic protein (MBP) immunodominant epitope in Lewis rat Palm-GpMBP(74-85) (Gp: guinea pig), which induced experimental autoimmune encephalomyelitisin vivo strongly increased the T cell proliferative responsein vitro. We extended this study to the human immunodominant epitope hMBP(83-99), synthesizing different lipophilic peptides bearing a hydrophobic chain linked through an amide or a C-C bond. To this aim, we developed a synthetic pathway for (±)-N-Fmoc-Ahd-OH (Ahd: 2-aminohexadecanoic acid) which was used to synthesize diastereomeric peptides which were successfully separated by reverse-phase high-performance liquid chromatography. MBP-specific T cell lines recognizing the immunodominant epitope hMBP(83-99) have been generated from patients affected by multiple sclerosis. Their proliferative response to the native peptide and to some lipoderivatives has been investigated. In contrast to the animal model, none of the investigated lipopeptides exhibited ‘superagonist’ activity. |
Databáze: | OpenAIRE |
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