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2013 RSC Bio-Organic Group Postgraduate Symposium Manchester Institute of Biotechnology, University of Manchester Thursday 11Th April 2013

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2013 RSC Bio-Organic Group Postgraduate Symposium Manchester Institute of Biotechnology, University of Manchester Thursday 11Th April 2013 2013 RSC Bio-Organic Group Postgraduate Symposium Manchester Institute of Biotechnology, University of Manchester Thursday 11th April 2013 10:15 Registration, coffee, poster set-up 10:55 Welcome 11:00 – 12:30 Sarah Lovelock (University of Manchester) Anabaena variabilis Phenylalanine Ammonia Lyase: An investigation into the catalytic mechanism and applications as a biocatalyst. Cristina Marculescu (University College London) The Development of a New Class of Maleimides as Reagents for Protein Modification Simge Davulcu (University of Bath) Catalytic conversion of unactivated nitriles into N-substituted amides Jon Ashley (National University of Singapore) Hybridised-SELEX: a capillary electrophoresis based method for maximising the number of aptamers screened 12:30 – 13:40 Lunch, poster session 13:40 – 15:10 Ryan Beattie (University of Bristol) A Versatile Synthetic Approach to Novel Deoxy Sugar Analogues Matthew Styles (University of Manchester) Tailoring Complex Natural Products by Altering the Biosynthetic Machinery that Builds Them Oscar Cascón (Cardiff University) Study of (+)-δ-cadinene synthase mechanism using farnesyl diphosphate analogues. John M. Wadsworth (University of Edinburgh) The natural product inhibitor myriocin displays a unique dual mode of action against serine palmitoyltransferase 15:10 – 15:45 Coffee, poster session 15:45 – 16:30 Plenary lecture: Prof. Nigel Scrutton, Manchester Institute of Biotechnology Addressing controversies in tunnelling and dynamics in enzyme catalysed H transfer 16:30 – 17:15 Prizes, refreshments 17:30 Close We are grateful to the following organisations for sponsoring this event: 1 Talk 1 Anabaena variabilis Phenylalanine Ammonia Lyase: An investigation into the catalytic mechanism and applications as a biocatalyst. Authors: Sarah Lovelock, Rachel Heath, Richard Lloyd and Nicholas Turner. Presenting author affiliation: University of Manchester Other affiliations: CoEBio3 O O PAL OH +NH3 OH R R -NH3 NH2 Figure 1: The amination of substituted cinnamic acids to yield L-amino acids is catalysed by phenylalanine ammonia lyase In Nature, the enzyme phenylalanine ammonia lyase (PAL) catalyses the deamination of L-phenylalanine to yield trans-cinnamic acid and ammonia.1 However, the reaction is reversible under conditions of high ammonia concentration and synthetically useful conversions in the amination direction can be obtained. PALs therefore represent potentially attractive biocatalysts for the synthesis of enantiomerically pure L- amino acids from substituted cinnamic acids and ammonia (figure 1). The broad use of PALs as biocatalysts for the synthesis of non-natural amino acids is currently limited by their relatively narrow substrate range. The application of eukaryotic PALs as biocatalysts for the amination of cinnamic acid analogues has been described previously.2 However, the activity of prokaryotic PALs towards non-natural substrates has not been investigated. The bacterial PAL from Anabaena variabilis(AvPAL) has recently received attention as a potential therapeutic enzyme for the metabolic disorder phenylketonuria.3 An available crystal structure of this enzyme makes it a suitable target for structure guided directed evolution.4 We have examined the activity and enantioselectivity of AvPAL towards a broad range of non-natural substrates and compared this activity with the eukaryotic PALs from the yeast Rhodotorula glutinis (RgPAL) and parsley Petroselinum crispum (PcPAL). AvPAL shows significantly higher activity towards a series of non-natural substrates than previously described eukaryotic PALs. Interestingly, some non-natural substrates also led to significant formation of D-amino acids and the catalytic mechanism has been investigated. Key references: (1) N. J. Turner, Curr. Opin.Chem. Bio., 2011, 15, 234; J. Ward and R. Wohlgemuth, Curr. Org. Chem, 2010, 14, 1914 (2) A. Gloge, J. Zón, Á. Kövári, L. Poppe, and J. Rétey, Chem. Eur. J., 2000, 6, 3386; C. Paizs, A. Katona and J. Rétey, Eur. J. Org. Chem, 2006, 5, 1113; A. Gloge, B. Langer, L. Poppe and J. Rétey, Arch. Biochem. Biophys., 1998, 359, 1; S. Bartsch and U. T. Bornscheuer P.E.D.S., 2010, 23, 929. (3) M. C. Moffitt, G. V. Louie, M. E. Bowman, J. Pence, J. P. Noel and B. S. Moore, Biochemistry, 2007, 46, 1004 (4) L. Wang, A. Gamez, H. Archer, E. E. Abola, C. N. Sakissian, P. Fitzpatrick, D. Wendt, Y. Zhang, M. Velard, J. Bliesath, S. M. Bell, J. F. Lemontt, C. R. Scriver and R. C. Stevens, J. Mol. Biol., 2008, 380, 623. 2 Talk 2 THE DEVELOPMENT OF A NEW CLASS OF MALEIMIDES AS REAGENTS FOR PROTEIN MODIFICATION Authors: Cristina Marculescu, Dr. James Baker, Dr. Rachel Morgan, Dr. Lyn Jones. Presenting author affiliation: University College London, 20 Gordon St., London, WC1H 0AJ. Other affiliations: Pfizer In 2009, the Baker group reported on the bromomaleimides as the first of a new class of reagents that could be efficiently used for the highly selective and reversible modification of cysteine and for the bridging of disulfide bonds in proteins.1,2,3 Aiming to prove that these transformations are not restricted to bromomaleimides, the present work presents a library of novel analogues, bearing different leaving groups on the double bond. By controlling the chemistry of this class of compounds we were able to tune properties such as selectivity, reactivity, solubility, and cross reactivity with reducing agents. Fig. 1 Mono- and disubstituted maleimide analogues. The utility of the novel monosubstitued analogues as protein labelling reagents was shown using a single cysteine mutant of protein Grb2 (L111C) as a model system. The disubstitued analogues were tested as cystine bridging reagents therefore the model system used was somatostatin, a 14-aminoacid peptide containing a disulfide bridge. A novel dual modification of peptides method will be presented. Fig. 2 Reactivity profiles of mono and di-substituted maleimides with the model systems. Key references: (1) Tedaldi, L. M.; Smith, M. E. B.; Nathani, R. I.; Baker, J. R., Chem. Commun. 2009, 6583. (2) Smith, M. E. B.; Schumacher, F. F.; Ryan, C. P.; Tedaldi, L. M.; Papaioannou, D.; Waksman, G.; Caddick, S.; Baker, J. R. J. Am. Chem. Soc. 2010, 132, 1960. (3) Schumacher, F. F.; Nobles, M.; Ryan, C. P.; Smith, M. E. B.; Tinker, A.; Caddick, S.; Baker, J. R. Bioconj. Chem. 2011, 22, 132. 3 Talk 3 Catalytic conversion of unactivated nitriles into N-substituted amides Authors: Simge Davulcu, Jonathan M J Williams Presenting author affiliation: University of Bath The amide bond is essential to sustain life, making up the peptide bonds in proteins such as enzymes. It is found in numerous natural products and biologically active molecules (Scheme 1). Despite their importance, no currently used industrial methods for constructing the amide bond are particularly “practical” or atom–efficient. Scheme 1. Amide bonds in natural products and biologically active molecules We have developed a zinc triflate and hydroxylamine hydrochloride catalysed methodolgy for direct conversion of unactivated nitriles into N-substituted amides (Scheme 2). The reaction proceeds in environmentally friendly water and provides a straightforward, atom-efficient methodology to synthesise secondary and tertiary amides from nitriles which is a rarely reported transformation in the literature. Scheme 2. Amide synthesis from nitriles and amines in water The zinc triflate in combination with hydroxylamine hydrochloride salt efficiently catalyses the direct conversion of unactivated nitriles into N-substituted amides with both primary and secondary amines. Possible mechanisms for this reaction are discussed and evidence for initial amidoxime and amidine formation pathways are reported. Isolated yields vary from 25-96%. Key references: (1) S. Davulcu, C. L. Allen, K. Milne and J. M. J. Williams, ChemCatChem 2013, 5, 435-438. (2) C. L. Allen and J. M. J. Williams, Chemical Society Reviews 2011, 40, 3405-3415. (3) C. J. Cobley, M. van den Heuvel, A. Abbadi and J. G. de Vries , Tetrahedron Letters 2000, 41, 2467-2470. 4 Talk 4 Hybridised-SELEX: a capillary electrophoresis based method for maximising the number of aptamers screened Authors: Jon Ashley, Sam Fong Yau Li Presenting author affiliation: Department of Chemistry, National University of Singapore, 3 Science Drive 3 Singapore 117543 Aptamers are ssDNA or ssRNA which specifically bind to biomolecules such as proteins, small molecules and even whole cells. DNA aptamers are usually selected from a library of random sequences using a method called Systematic evolution of ligands by exponential enrichment (SELEX) (Ellington and Szostak 1990). A number of post SELEX modifications have appeared in the literature to address the issues associated with the use of SELEX such as reducing the number of rounds of selection needed. Capillary electrophoresis based methods such as CE-SELEX and Non-SELEX are attractive alternatives due to the high separation efficiency, which can allow a selection to be carried out in <5 rounds. Also CE-SELEX and Non-SELEX are carried out in free solution removing the necessity to immobilize the target and allowing the aptamers to bind with the whole target (Mendonsa and Bowser 2004; Berezovski, Musheev et al. 2006). Moreover Non- SELEX removes the need for intermittent amplification reducing the likelihood of contamination. However due to the small sample sizes associated with CE, the number of sequences screened is limited, reducing the likely hood of finding aptamers with high binding affinity. In this research, we propose a
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