[The relationship between the structure of dermorphines and their thermoregulatory activity].
The effect of structural modifications in the molecule of dermorphin on the functional state of thermoregulation of rats under cold, neutral, and hot environment has been studied. Thermoregulatory and vasomotor activities of 43 peptides (fragments and analogs) were tested in comparison with dermorphin. The role of amino acid residues in the second, third, fourth, and sixth positions was studied. Different fragments of dermorphin molecule proved to underlie different types of thermoregulatory activity (the hypothermic effect was observed in the N-terminal tripeptide, while the N-terminal hexapeptide had the vasodilator activity), and targeted modification of dermorphin molecule makes it possible to separate the hypothermic, vasodilatory, and vasoconstrictive activities. It was proposed that dermorphin is the ligand not only for micro-opioid receptors.
Emel'ianova
T G
TG
Guzevatykh
L S
LS
Andreeva
L A
LA
Alfeeva
L Iu
LIu
Miasoedov
N F
NF
D000595:Amino Acid Sequence; D000818:Animals; D001831:Body Temperature; D001833:Body Temperature Regulation / Q000187:drug effects*; D008297:Male; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D018847:Opioid Peptides / Q000737:chemistry / Q000494:pharmacology; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology; D051381:Rats; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D018847:Opioid Peptides; D010446:Peptide Fragments; C030058:dermorphin