Abstract:
:The functional role of the C-terminal amide group (-CONH2) of the molluscan regulatory peptide FMRFamide has been examined in two sets of analogues based on FnLKFamide and FnLRFamide (nL = norleucine). In each series the amide group was replaced by -CONHCH3, -CON(CH3)2, -CONHNH2, -COOCH3, -CH2OH, and -COOH. The analogues were tested for their ability to bind to receptors in membranes from Helix aspersa circumoesophageal ganglia and for their biological effects on the isolated Helix heart. The results indicate i) that agonist activity, but not binding to the receptor, requires the presence of the amide carbonyl group; ii) the hydrogen atoms of the amide group are not essential either for binding or for agonist activity (the mono- and dimethylamides were more effective than the parent compounds on both counts); iii) the is more effective an agonist than is the amide in stimulating Helix heart.
journal_name
Peptidesjournal_title
Peptidesauthors
Geraghty RF,Irvine GB,Williams CH,Cottrell GAdoi
10.1016/0196-9781(94)90173-2subject
Has Abstractpub_date
1994-01-01 00:00:00pages
73-81issue
1eissn
0196-9781issn
1873-5169pii
0196-9781(94)90173-2journal_volume
15pub_type
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