Email this article Conformational Differences between Active Angiotensins and Their Inactive Precursors
- Authors: Solopova O.N.1, Pozdnyakova L.P.1, Varlamov N.E.1, Bokov M.N.1, Morozkina E.V.2, Yagudin Т.А.2, Sveshnikov P.G.1
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Affiliations:
- Russian Research Center for Molecular Diagnostics and Therapy
- Bach Institute of Biochemistry, Russian Academy of Sciences
- Issue: Vol 4, No 1 (2012)
- Pages: 74-77
- Section: Research Articles
- URL: https://actanaturae.ru/2075-8251/article/view/10636
- DOI: https://doi.org/10.32607/20758251-2012-4-1-74-77
- ID: 10636
Cite item
Abstract
The peptide conformation in the context of a protein polypeptide chain is influenced by proximal amino acid residues. However, the mechanisms of this interference remain poorly understood. We studied the conformation of angiotensins 1, 2 and 3, which are produced naturally in a sequential fashion from a precursor protein angiotensinogen and contain an identical peptide core structure. Using the example of angiotensins 1, 2 and 3, it was shown that similar amino acid sequences may have significant conformational differences in various molecules. In order to assess the conformational changes, we developed a panel of high-affinity mouse monoclonal antibodies against angiotensins 1, 2 and 3 and studied their cross-reactivity in indirect and competitive ELISAs. It was found that the conformations of inactive angiotensin1 and the corresponding fragment of angiotensinogen are similar; the same is true for the conformations of active angiotensins 2 and 3, whereas the conformations of homologous fragments in the active and inactive angiotensins differ significantly.
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About the authors
O. N. Solopova
Russian Research Center for Molecular Diagnostics and Therapy
Author for correspondence.
Email: solopova@msn.com
Russian Federation
L. P. Pozdnyakova
Russian Research Center for Molecular Diagnostics and Therapy
Email: solopova@msn.com
Russian Federation
N. E. Varlamov
Russian Research Center for Molecular Diagnostics and Therapy
Email: solopova@msn.com
Russian Federation
M. N. Bokov
Russian Research Center for Molecular Diagnostics and Therapy
Email: solopova@msn.com
Russian Federation
E. V. Morozkina
Bach Institute of Biochemistry, Russian Academy of Sciences
Email: solopova@msn.com
Russian Federation
Т. А. Yagudin
Bach Institute of Biochemistry, Russian Academy of Sciences
Email: solopova@msn.com
Russian Federation
P. G. Sveshnikov
Russian Research Center for Molecular Diagnostics and Therapy
Email: solopova@msn.com
Russian Federation
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