Dimerization of neurokinin A and B COOH-terminal heptapeptide fragments enhanced the selectivity for tachykinin receptor subtypes.
We have synthesized dimeric analogues of neurokinin A and B COOH-terminal heptapeptide fragments and evaluated their biological activities to contract isolated smooth muscle preparations of the guinea-pig ileum and rat vas deferens. The dimers were fairly active and showed two-fold increased selectivity for receptors in the guinea-pig ileum as compared with monomers. Extremely slow dissociation indicated a possible bivalent interaction between dimer and receptor.
Kodama
H
H
Laboratory of Biochemistry, Faculty of Science, Kyushu University, Fukuoka, Japan.
Shimohigashi
Y
Y
Sakaguchi
K
K
Waki
M
M
Takano
Y
Y
Yamada
A
A
Hatae
Y
Y
Kamiya
H
H
D000595:Amino Acid Sequence; D000818:Animals; D006168:Guinea Pigs; D007082:Ileum / Q000187:drug effects; D066298:In Vitro Techniques; D008297:Male; D008969:Molecular Sequence Data; D009119:Muscle Contraction / Q000187:drug effects; D015288:Neurokinin A / Q000494:pharmacology*; D015287:Neurokinin B / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011487:Protein Conformation; D051381:Rats; D017981:Receptors, Neurotransmitter / Q000187:drug effects*; D018039:Receptors, Tachykinin; D014649:Vas Deferens / Q000187:drug effects
D010446:Peptide Fragments; D017981:Receptors, Neurotransmitter; D018039:Receptors, Tachykinin; D015288:Neurokinin A; D015287:Neurokinin B; C056408:neurokinin A(4-10); C053213:neurokinin B (4-10)