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BioAssay: AID 217703

Affinity for vasopressin V2-receptor of porcine renal medullary membrane

As part of a program to design potent antidiuretic vasopressin antagonists and to define the minimum effective pharmacophore requirements for vasopressin (VP) antagonist activity, we studied the importance of the C-terminal tripeptide of a previously reported peptide antagonist of arginine-vasopressin (AVP,1). The proline residue at position 7 in AVP is proposed to impart a conformational more ..
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 Tested Compounds
 Tested Compounds
All(13)
 
 
Unspecified(13)
 
 
 Tested Substances
 Tested Substances
All(13)
 
 
Unspecified(13)
 
 
 Related BioAssays
 Related BioAssays
AID: 217703
Data Source: ChEMBL (215031)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-21
Modify Date: 2014-08-24

Data Table ( Complete ):           View All Data
Target
Sequence: RecName: Full=Vasopressin V2 receptor; Short=V2R; AltName: Full=AVPR V2; AltName: Full=Antidiuretic hormone receptor; AltName: Full=Renal-type arginine vasopressin receptor
Description ..   
Comment ..   

Gene:AVPR2     Conserved Domain     Related Protein 3D Structures     More BioActivity Data..
Tested Compounds:
Description:
Title: Potent vasopressin antagonists lacking the proline residue at position 7.

Abstract: As part of a program to design potent antidiuretic vasopressin antagonists and to define the minimum effective pharmacophore requirements for vasopressin (VP) antagonist activity, we studied the importance of the C-terminal tripeptide of a previously reported peptide antagonist of arginine-vasopressin (AVP,1). The proline residue at position 7 in AVP is proposed to impart a conformational constraint to the peptide backbone that is essential for V2-receptor agonist activity. Since the structure-activity relationships for VP agonists and antagonists are different, we investigated the effect of proline on antagonist activity, by synthesizing analogue 3 lacking this residue. This analogue was found to retain a high degree of antidiuretic antagonist activity. Since deletion of the Gly residue at position 9 of the antagonist did not adversely affect VP antagonist potency, several vasopressin antagonist analogues (4-7 and 9) that lacked both the Pro and Gly residues were also studied. These, too, were found to block vasopressin V2-receptor activity. Our results indicate that neither the proline nor glycine residues are essential for antagonism of the V2 receptor.
(PMID: 2940368)
Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Target Type: Target is a single protein chain
Assay Data Source: Scientific Literature
Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1K bind activity commentK bind activity commentString
2K bind standard flagK bind standard flagInteger
3K bind qualifierK bind qualifierString
4K bind published valueK bind published valueFloat
5K bind standard valueK bind standard valueFloat

Data Table (Concise)
Data Table ( Complete ):     View All Data
Classification
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