Abstract:
:Based on the importance of heat shock proteins (HSPs) in diseases such as cancer, Alzheimer's disease or malaria, inhibitors of these chaperons are needed. Today's state-of-the-art techniques to identify HSP inhibitors are performed in microplate format, requiring large amounts of proteins and potential inhibitors. In contrast, we have developed a miniaturized protein microarray-based assay to identify novel inhibitors, allowing analysis with 300 pmol of protein. The assay is based on competitive binding of fluorescence-labeled ATP and potential inhibitors to the ATP-binding site of HSP. Therefore, the developed microarray enables the parallel analysis of different ATP-binding proteins on a single microarray. We have demonstrated the possibility of multiplexing by immobilizing full-length human HSP90α and HtpG of Helicobacter pylori on microarrays. Fluorescence-labeled ATP was competed by novel geldanamycin/reblastatin derivatives with IC50 values in the range of 0.5 nM to 4 μM and Z(*)-factors between 0.60 and 0.96. Our results demonstrate the potential of a target-oriented multiplexed protein microarray to identify novel inhibitors for different members of the HSP90 family.
journal_name
J Biotechnoljournal_title
Journal of biotechnologyauthors
Schax E,Walter JG,Märzhäuser H,Stahl F,Scheper T,Agard DA,Eichner S,Kirschning A,Zeilinger Cdoi
10.1016/j.jbiotec.2014.03.006subject
Has Abstractpub_date
2014-06-20 00:00:00pages
1-9eissn
0168-1656issn
1873-4863pii
S0168-1656(14)00109-6journal_volume
180pub_type
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