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Drug Discovery


to the premature death of all blood cells. Human complement component 5 protein (C5) is a validat- ed drug target in an already available anti-C5 anti- body approved therapy. The objective of research, conducted by


Novartis, was to first obtain the small-molecule inhibitor of C5 complement protein as the new more potent therapy with identified and optimised mechanism of action. Growing crystals suitable for X-ray crystallogra-


phy was unsuccessful and cryo-EM had to be used in experiments to narrow in on the binding region of the protein (Figure 8)9


DDW


Hans Raaijmakers has been a structural biologist since 1993. He started his career as a structural biologist (EMBL Heidelberg, Universidade Nova in Lisboa, University of Utrecht). He then spent 14 years working in the fields of crystallography, drug design and modelling in pharma for Organon, Schering-Plough, MSD and Lead Pharma. Hans now specialises in the development of MicroED at ThermoFisher.


Dr Mazdak Radjainia is an expert in pharma cryo- EM with 15 years of experience in academia and industry. His present responsibilities in Thermo Fisher Scientific Pharma EM team include leading various strategic partnerships aimed at pharma customer enablement by streamlining gene-2-struc- ture workflows, particularly for difficult mem- brane proteins. His particular interest is in devel- oping transferable GPCR cryo-EM workflows as part of GPCR cryo-EM and drug design collabora- tion with Monash University. Further objectives cover increasing throughput, ease-of-use and amenability of small proteins for cryo-EM.


Dr Hervé-William Remigy completing his PhD in Biophysics at the Biozentrum at the University of Basel in 2001 focusing on the structural analysis of membrane protein complexes using Electron Microscopy (EM). He then worked on EM automation and developed Cryo-EM sample preparation by flash freezing. Since 2009 he has worked at Thermo Fisher Scientific and currently supports Pharma customers as a Business Development Manager.


Aleksandar Stefanovic has a scientific background in chemical crystallography. He is experienced in the development of pharma market sub-segments and new business models, with more than 25 years of extensive work in corporate operations, sales,


Drug Discovery World Winter 2019/20 15


marketing and business development in the analyt- ical pharma sector. Aleksandar’s present responsi- bility in Thermo Fisher Scientific is pharma market development and organisational growth in Europe, North America and the Asia Pacific region.


References 1 Liang, YL et al. Phase-plate cryo-EM structure of a class B GPCR-G-protein complex. Nature v. 546, p. 118-123 June 1, 2017. 2 Lau, Carus et al. J Physiol 596.7 (2018) pp 1107-1119. 3 Xu et al 2019. Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell 176, 702-715, Published: February 7, 2019. 4Wyllie et al. Preclinical candidate for the treatment of visceral leishmaniasis that acts through proteasome inhibition. PNAS May 7, 2019 116 (19) 9318-9323, published: April 8, 2019. 5Wei, Jia et al. An allosteric mechanism for potent inhibition of human ATP- citrate lyase. Nature 568, 566- 570 (2019). Published: April 3, 2019. 6 Scapin, G et al. Structure of the insulin receptor-insulin complex by single particle cryo-EM analysis. Nature 556, p. 122-125 April 5, 2018. 7 Lindner et al (2019). Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC polyomaviruses. Immunity 50, 668-676, 2019, Published: February 26, 2019. 8 Li, Wenfei et al. Structural basis for selective stalling of human ribosome nascent chain complexes by a drug-like molecule. Nature Structural & Molecular Biology, Vol 26, 501- 509. Published: June 2019. 9 Jendza, Keith et al. A small- molecule inhibitor of C5 complement protein. Nature Chemical Biology, Vol 15, 666- 668, July 2019.


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