Synthesis and biological activity of tuftsin and rigin derivatives containing monosaccharides or monosaccharide derivatives
| Autor: | Laura Biondi, Fernando Filira, Mati Fridkin, Marina Gobbo, S. Dagan, Raniero Rocchi, F. Cavaggion |
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| Rok vydání: | 1987 |
| Předmět: |
Glycosylation
Optical Rotation Stereochemistry Phagocytosis Tuftsin Mice Inbred Strains Biochemistry Binding Competitive chemistry.chemical_compound Mice Structure-Activity Relationship Monosaccharide Animals Receptors Immunologic chemistry.chemical_classification Tetrapeptide Macrophages Glycopeptides Biological activity Glutamine Aldose chemistry Female Indicators and Reagents Oligopeptides |
| Zdroj: | International journal of peptide and protein research. 29(2) |
| ISSN: | 0367-8377 |
| Popis: | Synthesis of some modified rigins is described in which either D-gluconic acid or 2-amino-2-deoxy-beta-D-glucopyranose have been linked to the parent molecule through amide bonds involving the alpha-amino function, alpha-carboxyl function or the gamma-amide function of glutamine in position 2. Glu2-rigin and D-gluconyl-Glu2-rigin have also been synthesized. Binding and phagocytosis assays have been carried out on the rigin derivatives and on some glycosylated tuftsin derivatives as well. Of all the tested peptides only rigin enhanced the phagocytic capacity of mouse peritoneal macrophages to the same extent as tuftsin. The peptides H-Thr-Lys-Pro-Arg-NH-Glc and N alpha-gluconyl-Gly-Glu-Pro-Arg-OH slightly enhanced phagocytosis. H-Thr[(alpha + beta)-O-glucosyl]-Lys-Pro-Arg-OH was found to displace 3H-tuftsin even better than tuftsin but lacked the ability to stimulate phagocytosis. |
| Databáze: | OpenAIRE |
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