sincalide and phenethylamine

sincalide has been researched along with phenethylamine* in 1 studies

Other Studies

1 other study(ies) available for sincalide and phenethylamine

Article	Year
2-Phenylethyl ester and 2-phenylethyl amide derivative analogues of the C-terminal hepta- and octapeptide of cholecystokinin. International journal of peptide and protein research, 1988, Volume: 32, Issue:5 Syntheses of analogues of the C-terminal octa- and heptapeptide of cholecystokinin are described. These analogues were obtained by replacing the C-terminal phenylalanine residue by 2-phenylethyl alcohol or by 2-phenylethylamine derivatives and by replacing the tryptophan residue by a D-tryptophan. The CCK-derivatives were tested for their ability to inhibit binding of labeled CCK-8 to rat pancreatic acini and to guinea pig brain membranes, and for their action on stimulation of amylase release from rat pancreatic acini. Some of these derivatives appeared to exhibit only part of the CCK-activity on amylase release, the D-Trp analogues behaving as CCK-antagonists. Topics: Amino Acid Sequence; Amylases; Animals; Biological Assay; Brain; Cell Membrane; Chemical Phenomena; Chemistry, Physical; Esters; Guinea Pigs; Molecular Sequence Data; Pancreas; Peptide Fragments; Phenethylamines; Rats; Sincalide; Structure-Activity Relationship	1988

Article

Year

2-Phenylethyl ester and 2-phenylethyl amide derivative analogues of the C-terminal hepta- and octapeptide of cholecystokinin.

International journal of peptide and protein research, 1988, Volume: 32, Issue:5

Syntheses of analogues of the C-terminal octa- and heptapeptide of cholecystokinin are described. These analogues were obtained by replacing the C-terminal phenylalanine residue by 2-phenylethyl alcohol or by 2-phenylethylamine derivatives and by replacing the tryptophan residue by a D-tryptophan. The CCK-derivatives were tested for their ability to inhibit binding of labeled CCK-8 to rat pancreatic acini and to guinea pig brain membranes, and for their action on stimulation of amylase release from rat pancreatic acini. Some of these derivatives appeared to exhibit only part of the CCK-activity on amylase release, the D-Trp analogues behaving as CCK-antagonists.

Topics: Amino Acid Sequence; Amylases; Animals; Biological Assay; Brain; Cell Membrane; Chemical Phenomena; Chemistry, Physical; Esters; Guinea Pigs; Molecular Sequence Data; Pancreas; Peptide Fragments; Phenethylamines; Rats; Sincalide; Structure-Activity Relationship

1988