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3 Polish Journal of Chemistry

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Lysine-Vasopressin Analogues with Glycoconjugates in Position 8

Marcinkowska A., Borovickova L., Slaninova J., Grzonka Z.

Polish Journal of Chemistry

2006

Vol. 80, nr 5

759-766

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.

Analogues of Arginine Vasopressin (AVP) Modified in the N-terminal Part of the Molecule with Stereoisomers of 4-Aminopyroglutamic Acid

Sobolewski D., Kowalczyk W., Derdowska I., Slaninova J., Kaczmarek K., Zabrocki J., Lammek B.

Polish Journal of Chemistry

2005

Vol. 79 / nr 4

731-737

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.

Analogues of Arginine Vasopressin (AVP) Modified in the N-Thermal Part of the Molecule with N-Benzylglycine

Jastrzębska B., Derdowska I., Kuncarowa P., Slaninova J., Lammek B., B. Olejniczak B., Zabrocki J.

Polish Journal of Chemistry

2002

Vol. 76 / nr 6

823-830

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.