Influence of the conformation of a macromolecule on the generation of T-cell proliferative response. A study with model polypeptides
| Autor: | E. Lacassie, Y. Trudelle, Agnès F. Delmas |
|---|---|
| Přispěvatelé: | Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), LEGOUPIL, Laëtitia |
| Rok vydání: | 1994 |
| Předmět: |
Proline
Protein Conformation T cell [SDV]Life Sciences [q-bio] T-Lymphocytes Molecular Sequence Data Biophysics Lymphocyte Activation Biochemistry Epitope 03 medical and health sciences Aggregation Epitopes Mice Structure-Activity Relationship 0302 clinical medicine Structural Biology Genetics medicine Animals Histone octamer Amino Acid Sequence Conformation Molecular Biology 030304 developmental biology Repeat unit 0303 health sciences Mice Inbred BALB C Chemistry Cell Biology Proliferative response [SDV] Life Sciences [q-bio] medicine.anatomical_structure T-cell epitope α-Helix Polypeptide Oligopeptides 030215 immunology Macromolecule |
| Zdroj: | FEBS Letters FEBS Letters, Wiley, 1994, 349 (3), pp.380-4 |
| ISSN: | 0014-5793 1873-3468 |
| Popis: | International audience; To study the influence of the conformation of polypeptidic macromolecules on the generation of T-cell epitopes, sequential polypeptides with an octamer repeat unit were designed and synthesized. They adopt mainly unordered and alpha-helical conformations. Among these polypeptides, those containing proline are fully or partly unordered, and are more effective at inducing T-cell proliferation than a proline-free very stable alpha-helical polypeptide. This extremely stable alpha-helical conformation, probably stabilized by aggregation, would enhance its stability against proteolytic processing. |
| Databáze: | OpenAIRE |
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