| Autor: | L. A. Andreeva, Miasoedov Nf, Kamenskiĭ Aa, A.P. Bonartsev, L. S. Guzevatykh, Emel'ianova Tg, L Iu Alfeeva, A. B. Usenko |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
chemistry.chemical_classification
Stereochemistry medicine.medical_treatment Intraperitoneal injection Peptide Dermorphin Thermoregulation General Biochemistry Genetics and Molecular Biology chemistry.chemical_compound Residue (chemistry) chemistry medicine Structure–activity relationship Proline General Agricultural and Biological Sciences Opioid peptide |
| Zdroj: | Biology Bulletin of the Russian Academy of Sciences. 29:284-289 |
| ISSN: | 1062-3590 |
| Popis: | We studied the influence of dermorphin (dermorphin) analogs with stereochemical modification of the amino acid residue proline in position 6 (Pro6), Tyr-D-Ala-Phe-Gly-Tyr-Hyp-Ser-NH2, Tyr-D-Ala-Phe-Gly-Tyr-[D-Pro]-Ser-NH2, Tyr-D-Ala-Phe-Gly-Tyr-[dehydro-Pro]-Ser-NH2, and Tyr-D-Ala-Phe-Gly-Tyr-[D-dehydro-Pro]-Ser-NH2, after their intraperitoneal injection at 0.5 mg/kg dose in the cold (4-7 degrees C), thermoneutral (27-28 degrees C), and hot (31-33 degrees C) environment. Stereochemical modifications of amino acid residue Pro6 proved to induce specific changes in the thermoregulatory effect of the peptide. Substitution of DPro6 for Pro6 has the most dramatic consequences: it considerably attenuates the thermoregulatory effect of dermorphin in the cold environment, cancels it in the hot environment, and inverts the dermorphin-specific thermoregulatory response in thermoneutral conditions. The data obtained indicate the important role of Pro6 residue in realization of this physiological activity of dermorphins. |
| Databáze: | OpenAIRE |
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