- Tytuł:
- Solution structure of conformationally restricted vasopressin analogues.
- Autorzy:
-
Trzepałka, Emilia
Oleszczuk, Marta
Maciejczyk, Maciej
Lammek, Bernard - Powiązania:
- https://bibliotekanauki.pl/articles/1043316.pdf
- Data publikacji:
- 2004
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
vasopressin
X-PLOR
NMR spectroscopy
EDMC
peptide conformation - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2004, 51, 1; 33-49
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł