Solid-phase synthesis and biological activity of the parallel dimer of deamino-oxytocin.
The parallel dimer of deamino-oxytocin has been synthesized by a novel solid-phase route. Successive orthogonal deprotection and oxidation reactions, carried out while the peptide remained anchored to a polymeric support, resulted in the formation of two disulfide bridges and conversion, with minimal side reactions, of the linear monomeric precursor to the dimer. The purified dimer showed approximately 0.1% to 2% of the biological activities of the monomer, as well as prolonged action. The time course of response to the deamino-oxytocin dimer differed from that of the monomer (and of oxytocin), and is probably due to slow formation of monomer under the conditions of biological testing.
Munson
M C
MC
Department of Chemistry, University of Minnesota, Minneapolis 55455.
Lebl
M
M
Slaninová
J
J
Barany
G
G
D000595:Amino Acid Sequence; D000818:Animals; D005260:Female; D008969:Molecular Sequence Data; D010120:Oxytocics / Q000138:chemical synthesis* / Q000494:pharmacology; D010121:Oxytocin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology; D010456:Peptides, Cyclic / Q000138:chemical synthesis* / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar; D014590:Uterine Contraction / Q000187:drug effects
D010120:Oxytocics; D010456:Peptides, Cyclic; C004748:deaminooxytocin; D010121:Oxytocin