Biological activity and receptor binding properties of some C-terminally modified analogues of FMRFamide.

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

Peptides

journal_title

Peptides

authors

Geraghty RF,Irvine GB,Williams CH,Cottrell GA

doi

10.1016/0196-9781(94)90173-2

subject

Has Abstract

pub_date

1994-01-01 00:00:00

pages

73-81

issue

1

eissn

0196-9781

issn

1873-5169

pii

0196-9781(94)90173-2

journal_volume

15

pub_type

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