[Opiate-like peptides with primary structure different from that of enkephalins].
Some new opiate-like peptides originating from opioid peptide precursors, dinorphine, histone H2b, major myeline protein, natriuretic atriopeptide and from the immunomodulating protein splenin whose primary structure differs essentially from that of enkephalins are described. Being intracysternally injected to mice, all the peptides under study caused a naloxone-sensitive analgetic effect as could be judged from the tail pinch tests. The effects of some opiate-like peptides were much stronger than that of leu-enkephalin. According to their primary structure, the opiate-like peptides can randomly be allocated into two families. Dipeptide Lys-Arg and free arginine also possess a marked analgetic activity which is abolished by naloxone. It seems likely that the epiate-like activity of the peptides under study is due to the similarity of their secondary and ternary structure to that of enkephalins of to their involvement in the regulation of opioid peptide metabolism.
Kharchenko
E P
EP
Kalikhevich
V N
VN
Sokolova
T V
TV
Shestak
K I
KI
Ardemasova
Z A
ZA
D000595:Amino Acid Sequence; D000700:Analgesics; D000818:Animals; D004723:Endorphins / Q000032:analysis* / Q000138:chemical synthesis / Q000494:pharmacology; D004745:Enkephalins / Q000032:analysis* / Q000494:pharmacology; D051379:Mice
D000700:Analgesics; D004723:Endorphins; D004745:Enkephalins
Printsipial'no otlichnye po pervichnoĭ strukture ot énkefalinov opiatopodobnye peptidy.