Dissociation of immunostimulant activities of muramyl dipeptide (MDP) by linking amino-acids or peptides to the glutaminyl residue
| Autor: | C. Damais, Pierre Lefrancier, Jean Choay, Francoise Audibert, Louis Chedid, M. Parant, M. Derrien |
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| Rok vydání: | 1980 |
| Předmět: |
Male
medicine.drug_class Stereochemistry medicine.medical_treatment Guinea Pigs Biophysics In Vitro Techniques Biochemistry Immunostimulant Dissociation (chemistry) Mice Structure-Activity Relationship chemistry.chemical_compound Residue (chemistry) Adjuvants Immunologic Glutamates medicine Animals Amino Acids Molecular Biology chemistry.chemical_classification Tetrapeptide Chemistry Glycopeptides Proteins Cell Biology Thymidine incorporation Amino acid carbohydrates (lipids) Female Acetylmuramyl-Alanyl-Isoglutamine Adjuvant Spleen Muramyl dipeptide Thymidine |
| Zdroj: | Biochemical and Biophysical Research Communications. 96:915-923 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(80)91442-4 |
| Popis: | N-acetyl-muramyl-L-alanyl-D-isoglutamine (muramyl dipeptide or MDP) is the minimal structure required for substituting mycobacteria in Freund's complete adjuvant. It is an adjuvant when injected in saline, protects mice non-specifically against infection, and enhances thymidine incorporation of lymphocytes. In this report it is shown that the linking of L-Lys, L-Ala-D-Ala, L-Lys-D-Ala or L-Lys-L-Ala to MDP permits the dissociation of anti-infectious activity from adjuvant activity. The optical configuration of the added residues plays the major role in this dissociation. It can be noted that the muramyl tetrapeptide MurNAc-L-Ala-D-isoGln-L-Lys-D-Ala mimicking the natural structure is devoid of anti-infectious activity. |
| Databáze: | OpenAIRE |
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