Two analogues of lysine-vasopressin in which the lysine side chain was modified by the attachment of glucuronic acid through the amide bond were synthesized and their pharmacological properties evaluated. In comparison to arginine-vasopressin used as a standard, both analogues were found to exhibit low activity in vasopressor test, moderate activity in antidiuretic test, and comparable activity in uterotonic test.
The present work is a part of our studies aimed at clarifying the influence of sterical constraints in N-terminal part of AVP analogues on the pharmacological activity of the resulting peptides. In this study we described the synthesis of four new analogues of AVP substituted at positions 2 and 3 or 3 and 4 with two diastereoisomers of 4-aminopyroglutamic acid and four peptides in which we combined the above modification with the placement of 3-mercaptopropionic acid at position 1. All new peptides were not active in bioassays for pressor, antidiuretic and uterotonic activity.
The synthesis and some pharmacological properties of five new analogues of arginine vasopressin (AVP) substituted with N-benzylglycine are described. All new peptides were tested for pressor and uterotonic activity. The results obtained imply that the structural change studied is in general incompatible with interaction of the analogues withV1A and OT receptors, however, in combination with suitable additional changes, may be of value in the design of new antagonists of these receptors.
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