Conformational Differences between Active Angiotensins and Their Inactive Precursors

نویسندگان

  • O.N. Solopova
  • L.P. Pozdnyakova
  • N.E. Varlamov
  • M.N. Bokov
  • E.V. Morozkina
  • Т.А. Yagudin
  • P.G. Sveshnikov
چکیده

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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عنوان ژورنال:

دوره 4  شماره 

صفحات  -

تاریخ انتشار 2012