NDLI: Direct monitoring of protein–protein inhibition using nano electrospray ionization mass spectrometry

Content Provider	Royal Society of Chemistry (RSC)
Author	Berg, Thorsten Hofmann, Daniela Cubrilovic, Dragana Wider, Gerhard Gräber, Martin Zenobi, Renato Barylyuk, Konstantin Walczak, Michal Jerzy
Copyright Year	2014
Abstract	Dissociation of the TNF-alpha trimer caused by the small-molecule inhibitor SPD304 was monitored using native ESI-MS and ion mobility spectrometry (IMS). Upon addition of the inhibitor, our data clearly indicate partial dissociation of the protein into dimers and monomers. The IMS-MS analysis shows that dimeric ions have their own characteristic drift time distributions, which are different from those of the dimer ions originating in the gas phase due to collision-induced dissociation. We show that only one equivalent of the inhibitor binds to the trimeric form. We also investigated inhibition of heterodimer formation of the survival protein Bcl-xL with the cell death-promoting regions of the proteins Bak and Bad, using the small inhibitors ABT737 and ABT263. We found that ABT737 is more potent than ABT263 in preventing the heterodimerization between Bcl-xL and the Bak and Bad derived BH3 peptides. We could also monitor the mode of binding, which in this case is competitive. These results indicate that native ESI-MS can be widely used to study the inhibition of other relevant protein–protein interactions (PPIs), and provide a good basis for further improvement and identification of small-molecule PPI inhibitors.
Starting Page	2794
Ending Page	2803
Page Count	10
File Format	HTM / HTML PDF
ISSN	20416520
Volume Number	5
Issue Number	7
Journal	Chemical Science
DOI	10.1039/c3sc53360c
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Protein trimer Tumor necrosis factor alpha Bcl-xL Spa town Collision-induced dissociation Enzyme inhibitor Ion Dissociative Protein dimer Bak Protein
Content Type	Text
Resource Type	Article
Subject	Chemistry

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