Structural determinants of the binding of gliadin fragments to human peripheral blood lymphocytes
| Autor: | Miklós Hollósi, László Gráf, G.D. Fasman, K. Medzihradszky, G. Kunos, H. Süli-Vargha |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Circular dichroism
Protein Conformation Molecular Sequence Data Peptide Gliadin Blood cell Cellular and Molecular Neuroscience Endocrinology Protein structure medicine Humans Amino Acid Sequence Lymphocytes Binding site Protein secondary structure chemistry.chemical_classification biology Naloxone Endocrine and Autonomic Systems Chemistry Circular Dichroism nutritional and metabolic diseases General Medicine Peptide Fragments digestive system diseases Solutions medicine.anatomical_structure Neurology Biochemistry biology.protein Endorphins Casomorphin |
| Zdroj: | Neuropeptides. 17:111-116 |
| ISSN: | 0143-4179 |
| Popis: | A series of alpha-gliadin fragments, structurally related to alpha-gliadin-(43-49), were synthesized. The effect of these fragments and beta-casomorphin and naloxone on the steady-state binding of [125I]-alpha-gliadin-(43-49) to human peripheral blood lymphocytes was investigated. In an attempt to correlate the binding data with the conformation of the peptides, their circular dichroism spectra were measured in both trifluorethanol and aqueous solution. It was found that there is a striking correlation between the results of the binding studies and the chiroptical properties of the gliadin fragments. The presence of N-terminal tyrosine and the tendency of the peptides to adopt periodic, 310 helix-like secondary structure appear to be crucial for the binding to human peripheral blood lymphocytes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|