The pleasant fact is that our activities cannot be summarised in a single blog entry any more! That is why we had to write two entries for 2014, this is the second one

In this part we wanted to bring up the exciting science at SARomics Biostructures.  Our experience has shown that running our own research and discovery projects both inside and outside the company is a prerequisite for the success of our CRO activity. While some of us are entirely focused on customers’ projects, on internal discovery projects and development of the technology platform, others combine company-related work with academic projects at Lund University, where they have PhD students and post-docs. All this together creates an exciting combination of science and business at the company.

Going back to 2014, one of the absolute highlights was getting the BIOCASCADE project funded by the EU. Within this project 11 early-stage researchers (normally called PhD students!) will investigate the development of sustainable chemo-enzymatic cascade reactions for the synthesis of optically pure amines and aminoalcohols as pharmaceutical ingredients. The project combines different techniques such as biocatalysis, transition-metal catalysis, compartmentalization, protein engineering and reaction engineering, in order to develop commercially viable and environmentally benign chemo-enzymatic reactions. SARomics Biostructures will participate in the consortium, together with 11 other partners, and contribute to the structure-based enzyme engineering part of the project. This will be our first commercial move into the field of industrial enzymology and we feel very excited about this new opportunity. Among the participants in the consortium are three SMEs (EntreChem, ENZYMICALS, ViaZym), seven university laboratories (Ruhr University Bochum and Greifswald University; Royal Institute of Technology, Stockholm; University of Oviedo; University of Amsterdam; Bielefeld University and Graz University of Technology) and DSM, a leading European chemical company.

Additional research highlights from 2014 include two publications co-authored by SARomics Biostructures staff, one by von Schantz et al. (2014) in which the recognition of xyloglucan by the carbohydrate binding module was studied. The second paper by Badarau et al. (2014) presented a study of heterodimer formation and receptor binding by the Staphylococcus aureus bi-component toxin LukGH. And of course we should not forget the review by Turnbull, Boyd and Walse on fragment-based discovery in targeting protein-protein interactions, which was highlighted in the Practical Fragments blog. For several reasons drug discovery efforts are increasingly turning to the area of protein-protein interactions, and the question of how fragment libraries should be designed for targeting PPI in the most optimal way is central for future progress in this direction. Luckily, the review was published online just in time for the FBLD 2014 meeting that took place in Basel in the end of September.

Coming back to the meeting-theme of the previous blog, the absolute highlight of our activities last autumn was the trip to Yokohama for the Bio-Japan partnering meeting in October. This is Japan’s primary event involving the global biotechnology industry. We participated in the Scandinavian pavilion organized by Business Sweden, Invest in Denmark and Medicon Valley Alliance. At the huge partnering event we met with several Japanese pharmaceutical companies and also made a presentation during the Scandinavian session within the conference programme. The trip to japan was not entirely devoted to the Bio-Japan meeting. Prior to the meeting SARomics was presented at a matchmaking seminar at the Danish Embassy in Tokyo for special invited guests. While being in Japan we also took the opportunity to make site visits to collaborators and to meet potential customers. Thus, it was both an exciting and productive trip.

We should also mention the PSDI (Protein Structure Determination in Industry) conference held from 2-5 November. The meeting was held in Portugal and nicely covered topics ranging from fragment based drug design to protein-protein complexes. A range of biophysical methods to study protein-ligand interactions were described, including recently developed techniques such as microscale capillary thermophoresis, but also more established methods like NMR, SPR and the Thermofluor technique that we use extensively in the lab. Interestingly, the Thermofluor technique seems to show good predictability for obtaining protein-ligand complex structures, which is something that we have also observed.

Publications:
von Schantz L, Håkansson M, Logan DT, Nordberg Karlsson E & Ohlin M (2014) Polar interactions with branching xyloses and CH-π interactions define carbohydrate binding module recognition of xyloglucan. Proteins, published online 10 Oct 2014, doi:10.1002/prot.24700

Badarau A, Rouha H, Malafa S, Logan DT, Håkansson M, Stulik L, Dolezilkova I, Teubenbacher A, Gross K, Maierhofer B, Weber S, Jägerhofer M, Hoffman D & Nagy E (2014) Structure-function analysis of heterodimer formation, oligomerization and receptor binding of the Staphylococcus aureus bi-component toxin LukGH. J. Biol. Chem., published online 3 Nov 2014, doi: 10.1074/jbc.M114.598110

Turnbull, A.P, Boyd, S.M. and Walse, B. (2014) Fragment-based drug discovery and protein-protein interactions. Research and Reports in Biochemistry, 4, 13-26.