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Findings from Institute of Pharmaceutical Science Yields New Findings on Biochemistry

May 27, 2014



By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Biochemistry have been presented. According to news reporting originating in Zurich, Switzerland, by NewsRx journalists, research stated, "The binding of epothilones to dimeric tubulin and to microtubules has been studied by means of biochemical and NMR techniques. We have determined the binding constants of epothilone A (EpoA) and B (EpoB) to dimeric tubulin, which are 4 orders of magnitude lower than those for microtubules, and we have elucidated the conformation and binding epitopes of EpoA and EpoB when bound to tubulin dimers and microtubules in solution."

The news reporters obtained a quote from the research from the Institute of Pharmaceutical Science, "The determined conformation of epothilones when bound to dimeric tubulin is similar to that found by X-ray crystallographic techniques for the binding of EpoA to the Tubulin/RB3/TTL complex; it is markedly different from that reported for EpoA bound to zinc-induced sheets obtained by electron crystallography. Likewise, only the X-ray structure of EpoA bound to the Tubulin/RB3/TTL complex at the luminal site, but not the electron crystallography structure, is compatible with the results obtained by STD on the binding epitope of EpoA bound to dimeric tubulin, thus confirming that the allosteric change (structuring of the M-loop) is the biochemical mechanism of induction of tubulin assembly by epothilones. TR-NOESY signals of EpoA bound to microtubules have been obtained, supporting the interaction with a transient binding site with a fast exchange rate (pore site), consistent with the notion that epothilones access the luminal site through the pore site, as has also been observed for taxanes."

According to the news reporters, the research concluded: "Finally, the differences in the tubulin binding affinities of a series of epothilone analogues has been quantitatively explained using the newly determined binding pose and the COMBINE methodology."

For more information on this research see: Molecular Recognition of Epothilones by Microtubules and Tubulin Dimers Revealed by Biochemical and NMR Approaches. ACS Chemical Biology, 2014;9(4):1033-1043. ACS Chemical Biology can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; ACS Chemical Biology - www.pubs.acs.org/journal/acbcct)

Our news correspondents report that additional information may be obtained by contacting A. Canales, Inst Pharmaceut Sci, Dept. of Chem & Appl Biosci, CH-8093 Zurich, Switzerland. Additional authors for this research include L. Nieto, J. Rodriguez-Salarichs, P.A. Sanchez-Murcia, C. Coderch, A. Cortes-Cabrera, I. Paterson, T. Carlomagno, F. Gago, J.M. Andreu, K.H. Altmann, J. Jimenez-Barbero and J.F. Diaz (see also Biochemistry).

Keywords for this news article include: Zurich, Europe, Macrolides, Switzerland, Biochemical, Epothilones, Biochemistry, Nanotechnology, Emerging Technologies, Molecular Recognition

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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