On the degradation of dermorphin and D-Arg2-dermorphin analogs by a soluble rat brain extract |
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Authors: | Y Sasaki M Hosono M Matsui H Fujita K Suzuki S Sakurada T Sakurada K Kisara |
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Affiliation: | 1. Department of Dermatology, The Affiliated Hospital of North Sichuan Medical College, Nanchong 637000, Sichuan, China;2. Department of Oncology Radiotherapy, Cancer Center, The Third Affiliated Hospital of Wenzhou Medical University, Wenzhou 325200, Zhejiang, China;3. Department of Dermatology, The First People''s Hospital of Lanzhou City, Lanzhou 730050, Gansu, China |
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Abstract: | Degradation of dermorphin, [D-Arg2]dermorphin and [D-Arg2, Gly3, Phe4]dermorphin in a soluble rat brain extract was examined. The former two heptapeptides were degraded in a similar fashion to produce corresponding N-terminal tetrapeptide as the main degradation product along with the parallel release of Tyr5, Pro6 and Ser7-NH2. Tyr-D-Arg-Phe-Gly showed a good enzymatic stability. When captopril, an angiotensin-converting enzyme inhibitor, was present in the incubation mixture, hydrolysis of the Gly4-Tyr5 bond was markedly suppressed and resulted in release of the corresponding N-terminal hexapeptide as the main degradation product. Combined use of captopril and amastatin, an aminopeptidase inhibitor, markedly suppressed the hydrolysis of these peptides. On the other hand, [D-Arg2, Gly3, Phe4]dermorphin was hydrolyzed easier than the other two heptapeptides and considerable amounts of Tyr1 and Phe4 were released after 20 hr incubation while the N-terminal tetrapeptide, Tyr-D-Arg-Gly-Phe, showed a good enzymatic stability. On the basis of these results, possible degradation pathways of these heptapeptides were discussed. |
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