Synthesis and some pharmacological properties of the 23-peptide 15-lysine-secretin-(5--27). Special role of the residue in position 15 in biological activity of the vasoactive intestinal polypeptide.
The 23-peptide 15-lysine-secretin-(5-27) [S(5-27)] was synthesized on an insoluble support. The residue in position 15 of secretin, aspartic acid, was replaced by lysine, which occupies that position in the vasoactive intestinal polypeptide (VIP), a member of the secretin family. The resulting analogue showed increased VIP-like activity on smooth muscle preparations and unaltered secretin-like activity on pancreatic juice secretion in the rat. The affinity of the new analogue was high-affinity secretin receptors in acinar cells from guinea pig pancreas was less than that of S(5-27) but was higher than that of S(5-27) for high-affinity VIP receptors in the same cells.
D000818:Animals; D005768:Gastrointestinal Hormones / Q000494:pharmacology*; D006168:Guinea Pigs; D066298:In Vitro Techniques; D009126:Muscle Relaxation / Q000187:drug effects; D009130:Muscle, Smooth / Q000187:drug effects; D010179:Pancreas / Q000187:drug effects / Q000378:metabolism; D051381:Rats; D011956:Receptors, Cell Surface / Q000187:drug effects; D012633:Secretin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014660:Vasoactive Intestinal Peptide / Q000494:pharmacology*
D005768:Gastrointestinal Hormones; D011956:Receptors, Cell Surface; D012633:Secretin; D014660:Vasoactive Intestinal Peptide