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Guetzoyan L.,University of Cambridge | Ingham R.J.,University of Cambridge | Nikbin N.,University of Cambridge | Rossignol J.,University of Cambridge | And 9 more authors.
MedChemComm | Year: 2014

A combination of conventional organic synthesis, remotely monitored flow synthesis and bioassay platforms, were used for the evaluation of novel inhibitors targeting bromodomains outside the well-studied bromodomain and extra terminal (BET) family, here exemplified by activity measurements on the bromodomain of BRD9 protein, a component of some tissue-specific SWi/SNF chromatin remodelling complexes. The Frontal Affinity Chromatography combined with Mass Spectrometry (FAC-MS) method proved to be reliable and results correlated well with an independent thermal shift assay. © 2014 the Partner Organisations.


Bailey M.J.,University of Surrey | Randall E.C.,National Physical Laboratory United Kingdom | Randall E.C.,University of Birmingham | Costa C.,University of Surrey | And 8 more authors.
Analytical Methods | Year: 2016

Liquid Extraction Surface Analysis (LESA) is a new, high throughput tool for ambient mass spectrometry. A solvent droplet is deposited from a pipette tip onto a surface and maintains contact with both the surface and the pipette tip for a few seconds before being re-aspirated. The technique is particularly suited to the analysis of trace materials on surfaces due to its high sensitivity and low volume of sample removal. In this work, we assess the suitability of LESA for obtaining detailed chemical profiles of fingerprints, oral fluid and urine, which may be used in future for rapid medical diagnostics or metabolomics studies. We further show how LESA can be used to detect illicit drugs and their metabolites in urine, oral fluid and fingerprints. This makes LESA a potentially useful tool in the growing field of fingerprint chemical analysis, which is relevant not only to forensics but also to medical diagnostics. Finally, we show how LESA can be used to detect the explosive material RDX in contaminated artificial fingermarks. © The Royal Society of Chemistry 2016.


Kramell A.,Martin Luther University of Halle Wittenberg | Porbeck F.,Advion Ltd | Kluge R.,Martin Luther University of Halle Wittenberg | Wiesner A.,Advion Ltd | Csuk R.,Martin Luther University of Halle Wittenberg
Journal of Mass Spectrometry | Year: 2015

We present a method requiring no sample preparation for the direct identification of indigoid colorants in tiny amounts in ancient historic fabrics using ASAP®-MS. Exact determinations were completed in less than 1 min. © 2015 John Wiley & Sons, Ltd.


Maple H.J.,UCB Celltech | Scheibner O.,Thermo Fisher Scientific | Baumert M.,Advion Ltd | Allen M.,Advion Ltd | And 4 more authors.
Rapid Communications in Mass Spectrometry | Year: 2014

RATIONALENon-covalent mass spectrometry (MS) offers considerable potential for protein-ligand screening in drug discovery programmes. However, there are some limitations with the time-of-flight (TOF) instrumentation typically employed that restrict the application of non-covalent MS in industrial laboratories. METHODSAn Exactive Plus EMR mass spectrometer was investigated for its ability to characterise non-covalent protein-small molecule interactions. Nano-electrospray ionisation (nanoESI) infusion was achieved with a TriVersa NanoMate. The transport multipole and ion lens voltages, dissociation energies and pressure in the Orbitrap™ were optimised. Native MS was performed, with ligand titrations to judge retention of protein-ligand interactions, serial dilutions of native proteins as an indication of sensitivity, and a heterogeneous protein analysed for spectral resolution. RESULTSInteractions between native proteins and ligands are preserved during analysis on the Exactive Plus EMR, with the binding affinities determined in good agreement with expected values. High spectral resolution allows baseline separation of adduct ions, which should improve the accuracy and limit of detection for measuring ligand interactions. Data are also presented showing baseline resolution of glycoforms of a highly glycosylated protein, allowing binding of a fragment molecule to be detected. CONCLUSIONSThe high sensitivity and spectral resolution achievable with the Orbitrap technology confer significant advantages over TOF mass spectrometers, and offer a solution to current limitations regarding throughput, data analysis and sample requirements. A further benefit of improved spectral resolution is the possibility of using heterogeneous protein samples such as glycoproteins for fragment screening. This would significantly expand the scope of applicability of non-covalent MS in the pharmaceutical and other industries. Copyright © 2014 John Wiley & Sons, Ltd.

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