Solution structure of conformationally restricted vasopressin analogues

• Autorzy: Trzepalka E. , Oleszczuk M. , Maciejczyk M. , Lammek B.
• Języki publikacji: EN

Abstrakty

EN

In recent years, a massive effort has been directed towards designing potent and selective antagonists of neurohypophyseal hormones substituted at position 3. Modi­fication of vasopressin at position 3 with 4,4'-biphenylalanine results in pharmaco­logically inactive analogues. Chemically, this substitution appears to vary only slightly from those previously made by us (1-Nal or 2-Nal), which afforded potent agonists of V2 receptors. In this situation, it seemed worthwhile to study the struc­ture of the analogues with 4,4-biphenylalanine (BPhe) at position 3 in aqueous solu­tion using NMR spectroscopy and total conformational analysis. This contribution is part of extensive studies aimed at understanding spatial structures of 3-substituted [Arg8 ]vasopressin analogues of different pharmacological properties. NMR data were used to calculate 3D structures for all the analogues using two methods, EDMC with the ECEPP/3 force field, and molecular dynamic with the simulated annealing (SA) algorithm. The structures obtained by the first method show a better fit between the NMR spectral evidence and the calculation for all the peptides.

Słowa kluczowe

EN

renal water excretion; 1-desamino-8-D-arginine vasopressin; peptide conformation; therapeutic agent; mammal; vasopressin; cardiovascular function; V2 receptor; hormone

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2004
• Tom: 51
• Numer: 1
• Opis fizyczny: p.33-49,fig.,ref.

Twórcy

autor

Trzepalka E.

• University of Gdansk, J.Sobieskiego 18, 80-952 Gdansk, Poland

autor

Oleszczuk M.

autor

Maciejczyk M.

autor

Lammek B.

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