Thermoregulatory Activity of Dermorphin Fragments |
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| Authors: | T G Emel'yanova N N Goryacheva L S Guzevatykh L A Andreeva L Yu Alfeeva N F Myasoedov |
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| Institution: | (1) Semenov Institute of Chemical Physics, Russian Academy of Sciences, ul. Kosygina 4, Moscow, 119991, Russia;(2) Institute of Molecular Genetics, Russian Academy of Sciences, pl. Kurchatova 46, Moscow, 123182, Russia |
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| Abstract: | We studied the effect of C-terminal truncation of the dermorphin (DM) molecule and analogs of its N-terminal tetrapeptide, DOrn2]-DM1–4, DArg2]-DM1–4, DAla4]-DM1–4, DArg2, DAla4]-DM1–4, Arg-DM1–4, Arg-DArg2]-DM1–4, Arg-DAla4]-DM1–4, and Arg-DArg2, DAla4]-DM1–4, on the functional status of the thermoregulation system in rats at different ambient temperatures. For the first time, we demonstrate that the N-terminal tetrapeptide is the minimal fragment with the hypothermic effect. Only the N-terminal octapeptide exerted the vasomotor effect. Amino acid substitutions in the tetrapeptide affected its hypothermic effect. DArg2]-DM1–4 and DArg2, DAla4]-DM1–4 had the greatest effect. Addition of Arg to the N-terminus of DM1–4 analogs changed their thermoregulatory activity. The greatest thermoregulatory effect was observed for Arg-DArg2]-DM1–4 and Arg-DArg2, DAla4]-DM1–4. |
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