Use of electrospray mass spectroscopy for studying supramolecular interactions with proteins
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PERRET, Florent; COLEMAN, Anthony. Use of electrospray mass spectroscopy for studying supramolecular interactions with proteins. In: Physical Methods in Coordination and Supramolecular Chemistry. XVII, 27 septembrie - 1 octombrie 2006, Chişinău. Chisinau, Republic of Moldova: 2006, p. 67. ISBN 978-9975-62-066-6.
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Physical Methods in Coordination and Supramolecular Chemistry
XVII, 2006
Conferința "The XV-th International Conference Physical Methods in Coordination and Supramolecular Chemistry : The XVII-th Reading in memory of Acad. A.Ablov"
Chişinău, Moldova, 27 septembrie - 1 octombrie 2006

Use of electrospray mass spectroscopy for studying supramolecular interactions with proteins


Pag. 67-67

Perret Florent, Coleman Anthony
 
Institut de Biologie et Chimie des Protéines
 
Disponibil în IBN: 9 iunie 2020


Rezumat

Investigation of supramolecular interactions with proteins is of great interest in order to synthesize supramolecular host systems that will bind specifically, and inhibit or activate the protein. Mass spectroscopy has been used as a method allowing the determination of both the association constants and the binding stoichiometries of such protein- supramolecule interactions. Soft Ionisation mass spectrometric methods including MALDI and Electrospray Ionisation (ESI) are particularly well suited to the study of non-covalent complexes of biomolecules and macrocycle molecule. The complexation between water soluble calixarene derivatives and Bovine Serum Albumin has been undertaken by this method.figureFigure 1. View of mass spectra of BSA alone (a) and the complexing of BSA with 1b (b) at molar ratio 1:3 BSA/Calixarene after deconvolution. At this molar ratio, BSA is present as the uncomplexed form (p) and the complexed forms with one molecule of 1b (£) and with two molecules of 1b (™). It has been demonstrated by a wide body of work that the association constants obtained by the method used are an accurate reflection of those observed in solution. The observed association constants are in the range 104-106 M-1. As it has been previously noted for other organic anions three binding sites may be present. The strength of binding varies inversely with the size of the parasulphonatocalix[n]arenes. Other experiments on complexation between water soluble calixarenes and other proteins (NBD1 for example) are currently being undertaken.