Synthetic homo-oligomethionine chemoattractants
| Autor: | Gian Maria Bonora, Elmer L. Becker, Claudio Toniolo, Claudio Bismara, Richard J. Freer |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
chemistry.chemical_classification
Circular dichroism Oligopeptide Dipeptide Chemotactic Factors Spectrophotometry Infrared Neutrophils Protein Conformation Stereochemistry Circular Dichroism Peptide In Vitro Techniques Biochemistry Chemotaxis Leukocyte Structure-Activity Relationship chemistry.chemical_compound Methionine Enzyme chemistry Amide Animals Rabbits Receptor Oligopeptides Cytochalasin B |
| Zdroj: | International Journal of Peptide and Protein Research. 26:482-492 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1985.tb01015.x |
| Popis: | Using solution methods, we have synthesized several series of L-methionine homo-oligopeptides from the dipeptide to the hexapeptide with either a free alpha-carboxyl function or different C-blocking groups (methoxy, benzyloxy, benzylamino) and with N-blocking groups of either the amide type (formyl, pivaloyl) or the urethane type (tert.-butyloxycarbonyl). Compounds were compared to determine the combined effect of main-chain length and presence and nature of N- and C-blocking groups on conformation-activity relationship. Each peptide was tested for its ability to induce rabbit peritoneal polymorphonuclear leukocytes in the presence of cytochalasin B to secrete granule enzymes. In parallel, a conformational analysis was carried out in the solid state and in solution, using infrared absorption and circular dichroism. The biological and conformational data are discussed in relation to a recently proposed model of the chemotactic peptide receptor of rabbit neutrophils. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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