Dr Drew Thomson

  • Lecturer (School of Chemistry)

telephone: 01413308284
email: Drew.Thomson@glasgow.ac.uk

Room A3-15, Joesph Black Building, School of Chemistry, G12 8QQ

ORCID iDhttps://orcid.org/0000-0002-1066-1369

Biography

Drew Thomson

I started my independent career as a Lecturer in Chemical Biology at Glasgow in 2016. Before this I studied for an MChem degree at University of Edinburgh, where I then stayed for a PhD in supramolecular organic chemistry in the group of Prof David Leigh. After a short postdoc in protein biophysics (also in Edinburgh) in the group of Dr David Dryden, I moved to Bristol, as a postdoc and later research fellow, in the lab of Prof Dek Woolfson, working on peptide design and synthesis. The Thomson group now works on combining all these disparate influences to understand and design peptides in chemical biology.

Outside of research, I am enthusiastic about widening participation in chemistry. I am now the Athena SWAN lead for Chemistry at University of Glasgow, and am keen to learn about, discuss, promote and help with any activities around EDI in science.

Publications

Google Scholar link to Drew's publications

Reviewing

I review regularly for RSC and ACS journals, and am always keen to review manuscripts at the chemistry/biology interface, and especially in the peptide chemistry and chemical biology spheres. I am a member of the EPSRC College, and review grant applications from EPSRC, BBSRC and MRC, as well as the RSC and Leverhulme Trust.

Work with us

All of our funded studentship positions are filled at the moment. If you have, or are applying for, your own PhD or postdoctoral fellowship funding and are looking for a host group please do get in contact. We are happy to support applications for individual funding.

 

Research interests

Overview

Research in our lab is aimed at designing peptides with defined 3D conformations. We use these peptides to ask questions about biological systems, and to mimic behaviour seen in biology. By designing these molecules from first principles, we learn about the fundamental factors that govern the relationship between atomic connectivity and three-dimensional structure. Work in this area is necessarily multidisciplinary: our lab uses a mix of bioinformatics, computational modelling, peptide and organic synthesis, and biophysical characterisation. Our lab has all the resources needed for the synthesis, purification, and analysis of peptides, as well as resources and expertise in computational design and modelling. We are always interested to discuss potential collaborations! If you have a research question that could benefit peptide synthesis or design then please do get in contact.

Research Projects

Some of the projects we are currently researching in the Thomson lab:

Non-native Chemical Ligation

We have recently become interested in mimicking aspects of protein structure using the residual chemical functionality from a ligation reaction. This allows us to construct a beta turn mimic at the same time as carrying out a ligation reaction. In doing so, we generate a peptide which contains a non-natural unit, but which replicates the structural role of the residues that it has replaced. We are now expanding this method beyond beta turns to other linking units, and are investigating using these turn mimics as a way of adding extra chemical functionality to a peptide/protein mimic.

Cyclic Peptide Conformational Design

Cyclic peptides are an interesting sub-category of peptide because they are often exhibit fewer conformations than their linear counterparts. For this reason they have a lot of potential as bioactive molecules for research in Chemical Biology. However, designing a peptide sequence so that a cyclic peptide adopts a particular conformation is still a challenging task. We are investigating methods to address this challenge, and are testing these methods by developing cyclic peptides that mimic known binding loops in natural systems.

Computational Protein Design

We are generally interested in computational methods that can simplify the challenge of understanding the otherwise often bewildering behaviour of peptides and proteins. In particular, we are particularly interested in protein systems such as beta hairpins, collagen-like peptide, alpha helical coiled coils and others, where the geometry of the peptide can be described using comparatively few parameters. This allows us to use computer models to design and test new structural variants. We are contributors to the "Isambard" Python module for peptide/protein design and analysis.

Hybrid Peptide Biomaterials

Nature uses peptides/proteins for a range of structural roles, and there is a great deal yet to be learned about how these evolved materials. As part of a project with the LifETIME CDT, we are working with the group of Dr Bernhard Schmidt to investigate new peptide/polymer hybrid materials as scaffolds for cell engineering.

Research units

Publications

List by: Type | Date

Jump to: 2021 | 2020 | 2019 | 2018 | 2017 | 2016 | 2015 | 2014 | 2012 | 2011 | 2009 | 2008 | 2006
Number of items: 32.

2021

Rhys, G. G., Dawson, W. M., Beesley, J. L., Martin, F. J.O., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2021) How coiled-coil assemblies accommodate multiple aromatic residues. Biomacromolecules, 22(5), pp. 2010-2019. (doi: 10.1021/acs.biomac.1c00131) (PMID:33881308)

2020

Crecente Garcia, S., Neckebroeck, A., Clark, J. S. , Smith, B. O. and Thomson, A. R. (2020) β-turn mimics by chemical ligation. Organic Letters, 22(11), pp. 4424-4428. (doi: 10.1021/acs.orglett.0c01427) (PMID:32406695) (PMCID:PMC7304061)

2019

Rhys, G. G., Wood, C. W., Beesley, J. L., Zaccai, N. R., Burton, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2019) Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society, 141(22), pp. 8787-8797. (doi: 10.1021/jacs.8b13354) (PMID:31066556)

2018

Rhys, G. G., Wood, C. W., Lang, E. J.M., Mulholland, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2018) Maintaining and breaking symmetry in homomeric coiled-coil assemblies. Nature Communications, 9(1), 4132. (doi: 10.1038/s41467-018-06391-y) (PMID:30297707) (PMCID:PMC6175849)

Heal, J. W., Bartlett, G. J., Wood, C. W., Thomson, A. R. and Woolfson, D. N. (2018) Applying graph theory to protein structures: an atlas of coiled coils. Bioinformatics, 34(19), pp. 3316-3323. (doi: 10.1093/bioinformatics/bty347) (PMID:29722888)

Lommel, M. et al. (2018) Hydra mesoglea proteome identifies thrombospondin as a conserved component active in head organizer restriction. Scientific Reports, 8, 11753. (doi: 10.1038/s41598-018-30035-2) (PMID:30082916) (PMCID:PMC6079037)

2017

Wood, C. W., Heal, J. W., Thomson, A. R. , Bartlett, G. J., Ibarra, A. A., Brady, R. L., Sessions, R. B. and Woolfson, D. N. (2017) ISAMBARD: an open-source computational environment for biomolecular analysis, modelling and design. Bioinformatics, 33(19), pp. 3043-3050. (doi: 10.1093/bioinformatics/btx352) (PMID:28582565) (PMCID:PMC5870769)

Niitsu, A., Heal, J. W., Fauland, K., Thomson, A. R. , Woolfson, D. N. and Thomson, A. (2017) Membrane-spanning α-helical barrels as tractable protein-design targets. Philosophical Transactions of the Royal Society B: Biological Sciences, 372(1726), 20160213. (doi: 10.1098/rstb.2016.0213) (PMID:28630153)

Small, L. S.R., Bruning, M., Thomson, A. R. , Boyle, A. L., Davies, R. B., Curmi, P. M.G., Forde, N. R., Linke, H., Woolfson, D. N. and Bromley, E. H.C. (2017) Construction of a chassis for a tripartite protein-based molecular motor. ACS Synthetic Biology, 6(6), pp. 1096-1102. (doi: 10.1021/acssynbio.7b00037) (PMID:28221767) (PMCID:PMC5477008)

Mahendran, K. R., Niitsu, A., Kong, L., Thomson, A. R. , Sessions, R. B., Woolfson, D. N. and Bayley, H. (2017) A monodisperse transmembrane α-helical peptide barrel. Nature Chemistry, 9(5), pp. 411-419. (doi: 10.1038/nchem.2647) (PMID:28430192)

2016

Burton, A. J., Thomson, A. R. , Dawson, W. M., Brady, R. L. and Woolfson, D. N. (2016) Installing hydrolytic activity into a completely de novo protein framework. Nature Chemistry, 8(9), pp. 837-844. (doi: 10.1038/nchem.2555) (PMID:27554410)

Thomas, F., Burgess, N. C., Thomson, A. R. and Woolfson, D. N. (2016) Controlling the assembly of coiled-coil peptide nanotubes. Angewandte Chemie (International Edition), 55(3), pp. 987-991. (doi: 10.1002/anie.201509304) (PMID:26663438) (PMCID:PMC4744968)

2015

Burgess, N. C., Sharp, T. H., Thomas, F., Wood, C. W., Thomson, A. R. , Zaccai, N. R., Brady, R. L., Serpell, L. C. and Woolfson, D. N. (2015) Modular design of self-assembling peptide-based nanotubes. Journal of the American Chemical Society, 137(33), pp. 10554-10562. (doi: 10.1021/jacs.5b03973) (PMID:26219086)

Woolfson, D. N., Bartlett, G. J., Burton, A. J., Heal, J. W., Niitsu, A., Thomson, A. R. and Wood, C. W. (2015) De novo protein design: how do we expand into the universe of possible protein structures? Current Opinion in Structural Biology, 33, pp. 16-26. (doi: 10.1016/j.sbi.2015.05.009) (PMID:26093060)

Fletcher, J. M. et al. (2015) A basis set of de novo coiled-coil peptide oligomers for rational protein design and synthetic biology. ACS Synthetic Biology, 1(6), pp. 240-250. (doi: 10.1021/sb300028q) (PMID:23651206)

Mehrban, N. et al. (2015) Functionalized α-helical peptide hydrogels for neural tissue engineering. ACS Biomaterials Science and Engineering, 1(6), pp. 431-439. (doi: 10.1021/acsbiomaterials.5b00051) (PMID:26240838) (PMCID:PMC4517957)

2014

Bishop, P., Rubin, P., Thomson, A. R. , Rocca, D. and Henley, J. M. (2014) The ubiquitin C-terminal hydrolase L1 (UCH-L1) C terminus plays a key role in protein stability, but its farnesylation is not required for membrane association in primary neurons. Journal of Biological Chemistry, 289(52), pp. 36140-36149. (doi: 10.1074/jbc.M114.557124) (PMID:25326379) (PMCID:PMC4276877)

Wood, C. W., Bruning, M., Ibarra, A. Á., Bartlett, G. J., Thomson, A. R. , Sessions, R. B., Brady, R. L. and Woolfson, D. N. (2014) CCBuilder: an interactive web-based tool for building, designing and assessing coiled-coil protein assemblies. Bioinformatics, 30(21), pp. 3029-3035. (doi: 10.1093/bioinformatics/btu502) (PMID:25064570) (PMCID:PMC4201159)

Thomson, A. R. , Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L. and Woolfson, D. N. (2014) Computational design of water-soluble α-helical barrels. Science, 346(6208), pp. 485-488. (doi: 10.1126/science.1257452) (PMID:25342807)

Mehrban, N., Abelardo, E., Wasmuth, A., Hudson, K. L., Mullen, L. M., Thomson, A. R. , Birchall, M. A. and Woolfson, D. N. (2014) Assessing cellular response to functionalized α-helical peptide hydrogels. Advanced Healthcare Materials, 3(9), pp. 1387-1391. (doi: 10.1002/adhm.201400065) (PMID:24659615) (PMCID:PMC4276410)

2012

Sharp, T. H., Bruning, M., Mantell, J., Sessions, R. B., Thomson, A. R. , Zaccai, N. R., Brady, R. L., Verkade, P. and Woolfson, D. N. (2012) Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design. Proceedings of the National Academy of Sciences of the United States of America, 109(33), pp. 13266-13271. (doi: 10.1073/pnas.1118622109) (PMID:22847414) (PMCID:PMC3421226)

Woolfson, D. N., Bartlett, G. J., Bruning, M. and Thomson, A. R. (2012) New currency for old rope: from coiled-coil assemblies to α-helical barrels. Current Opinion in Structural Biology, 22(4), pp. 432-441. (doi: 10.1016/j.sbi.2012.03.002) (PMID:22445228)

2011

Zaccai, N. R. et al. (2011) A de novo peptide hexamer with a mutable channel. Nature Chemical Biology, 7(12), pp. 935-941. (doi: 10.1038/nchembio.692) (PMID:22037471) (PMCID:PMC3223406)

Mahmoud, Z. N., Gunnoo, S. B., Thomson, A. R. , Fletcher, J. M. and Woolfson, D. N. (2011) Bioorthogonal dual functionalization of self-assembling peptide fibers. Biomaterials, 32(15), pp. 3712-3720. (doi: 10.1016/j.biomaterials.2010.12.002) (PMID:21353303)

2009

Stephanou, A. S., Roberts, G. A., Cooper, L. P., Clarke, D. J., Thomson, A. R. , MacKay, C. L., Nutley, M., Cooper, A. and Dryden, D. T.F. (2009) Dissection of the DNA mimicry of the bacteriophage T7 Ocr protein using chemical modification. Journal of Molecular Biology, 391(3), pp. 565-576. (doi: 10.1016/j.jmb.2009.06.020) (PMID:19523474) (PMCID:PMC2806950)

Armstrong, C. T., Boyle, A. L., Bromley, E. H.C., Mahmoud, Z. N., Smith, L., Thomson, A. R. and Woolfson, D. N. (2009) Rational design of peptide-based building blocks for nanoscience and synthetic biology. Faraday Discussions, 143, pp. 305-317. (doi: 10.1039/B901610D) (PMID:20334109)

Leigh, D. A., Lusby, P. J., McBurney, R. T., Morelli, A., Slawin, A. M.Z., Thomson, A. R. and Walker, D. B. (2009) Getting harder: cobalt (III)-template synthesis of catenanes and rotaxanes. Journal of the American Chemical Society, 131(10), pp. 3762-3771. (doi: 10.1021/ja809627j) (PMID:19275264)

Bromley, E. H.C., Sessions, R. B., Thomson, A. R. and Woolfson, D. N. (2009) Designed α-helical tectons for constructing multicomponent synthetic biological systems. Journal of the American Chemical Society, 131(3), pp. 928-930. (doi: 10.1021/ja804231a) (PMID:19115943)

2008

Leigh, D. A. and Thomson, A. R. (2008) An ammonium/bis-ammonium switchable molecular shuttle. Tetrahedron Letters, 64(36), pp. 8411-8416. (doi: 10.1016/j.tet.2008.05.130)

Dryden, D. T.F., Thomson, A. R. and White, J. H. (2008) How much of protein sequence space has been explored by life on Earth? Journal of the Royal Society: Interface, 5(25), pp. 953-956. (doi: 10.1098/rsif.2008.0085) (PMID:18426772) (PMCID:PMC2459213)

2006

Leigh, D. A. and Thomson, A. R. (2006) Switchable dual binding mode molecular shuttle. Organic Letters, 8(23), pp. 5377-5379. (doi: 10.1021/ol062284j) (PMID:17078722)

Aucagne, V., Leigh, D. A., Lock, J. S. and Thomson, A. R. (2006) Rotaxanes of cyclic peptides. Journal of the American Chemical Society, 128(6), pp. 1784-1785. (doi: 10.1021/ja057206q) (PMID:16464065)

This list was generated on Fri Jul 30 21:11:44 2021 BST.
Jump to: Articles
Number of items: 32.

Articles

Rhys, G. G., Dawson, W. M., Beesley, J. L., Martin, F. J.O., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2021) How coiled-coil assemblies accommodate multiple aromatic residues. Biomacromolecules, 22(5), pp. 2010-2019. (doi: 10.1021/acs.biomac.1c00131) (PMID:33881308)

Crecente Garcia, S., Neckebroeck, A., Clark, J. S. , Smith, B. O. and Thomson, A. R. (2020) β-turn mimics by chemical ligation. Organic Letters, 22(11), pp. 4424-4428. (doi: 10.1021/acs.orglett.0c01427) (PMID:32406695) (PMCID:PMC7304061)

Rhys, G. G., Wood, C. W., Beesley, J. L., Zaccai, N. R., Burton, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2019) Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society, 141(22), pp. 8787-8797. (doi: 10.1021/jacs.8b13354) (PMID:31066556)

Rhys, G. G., Wood, C. W., Lang, E. J.M., Mulholland, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. (2018) Maintaining and breaking symmetry in homomeric coiled-coil assemblies. Nature Communications, 9(1), 4132. (doi: 10.1038/s41467-018-06391-y) (PMID:30297707) (PMCID:PMC6175849)

Heal, J. W., Bartlett, G. J., Wood, C. W., Thomson, A. R. and Woolfson, D. N. (2018) Applying graph theory to protein structures: an atlas of coiled coils. Bioinformatics, 34(19), pp. 3316-3323. (doi: 10.1093/bioinformatics/bty347) (PMID:29722888)

Lommel, M. et al. (2018) Hydra mesoglea proteome identifies thrombospondin as a conserved component active in head organizer restriction. Scientific Reports, 8, 11753. (doi: 10.1038/s41598-018-30035-2) (PMID:30082916) (PMCID:PMC6079037)

Wood, C. W., Heal, J. W., Thomson, A. R. , Bartlett, G. J., Ibarra, A. A., Brady, R. L., Sessions, R. B. and Woolfson, D. N. (2017) ISAMBARD: an open-source computational environment for biomolecular analysis, modelling and design. Bioinformatics, 33(19), pp. 3043-3050. (doi: 10.1093/bioinformatics/btx352) (PMID:28582565) (PMCID:PMC5870769)

Niitsu, A., Heal, J. W., Fauland, K., Thomson, A. R. , Woolfson, D. N. and Thomson, A. (2017) Membrane-spanning α-helical barrels as tractable protein-design targets. Philosophical Transactions of the Royal Society B: Biological Sciences, 372(1726), 20160213. (doi: 10.1098/rstb.2016.0213) (PMID:28630153)

Small, L. S.R., Bruning, M., Thomson, A. R. , Boyle, A. L., Davies, R. B., Curmi, P. M.G., Forde, N. R., Linke, H., Woolfson, D. N. and Bromley, E. H.C. (2017) Construction of a chassis for a tripartite protein-based molecular motor. ACS Synthetic Biology, 6(6), pp. 1096-1102. (doi: 10.1021/acssynbio.7b00037) (PMID:28221767) (PMCID:PMC5477008)

Mahendran, K. R., Niitsu, A., Kong, L., Thomson, A. R. , Sessions, R. B., Woolfson, D. N. and Bayley, H. (2017) A monodisperse transmembrane α-helical peptide barrel. Nature Chemistry, 9(5), pp. 411-419. (doi: 10.1038/nchem.2647) (PMID:28430192)

Burton, A. J., Thomson, A. R. , Dawson, W. M., Brady, R. L. and Woolfson, D. N. (2016) Installing hydrolytic activity into a completely de novo protein framework. Nature Chemistry, 8(9), pp. 837-844. (doi: 10.1038/nchem.2555) (PMID:27554410)

Thomas, F., Burgess, N. C., Thomson, A. R. and Woolfson, D. N. (2016) Controlling the assembly of coiled-coil peptide nanotubes. Angewandte Chemie (International Edition), 55(3), pp. 987-991. (doi: 10.1002/anie.201509304) (PMID:26663438) (PMCID:PMC4744968)

Burgess, N. C., Sharp, T. H., Thomas, F., Wood, C. W., Thomson, A. R. , Zaccai, N. R., Brady, R. L., Serpell, L. C. and Woolfson, D. N. (2015) Modular design of self-assembling peptide-based nanotubes. Journal of the American Chemical Society, 137(33), pp. 10554-10562. (doi: 10.1021/jacs.5b03973) (PMID:26219086)

Woolfson, D. N., Bartlett, G. J., Burton, A. J., Heal, J. W., Niitsu, A., Thomson, A. R. and Wood, C. W. (2015) De novo protein design: how do we expand into the universe of possible protein structures? Current Opinion in Structural Biology, 33, pp. 16-26. (doi: 10.1016/j.sbi.2015.05.009) (PMID:26093060)

Fletcher, J. M. et al. (2015) A basis set of de novo coiled-coil peptide oligomers for rational protein design and synthetic biology. ACS Synthetic Biology, 1(6), pp. 240-250. (doi: 10.1021/sb300028q) (PMID:23651206)

Mehrban, N. et al. (2015) Functionalized α-helical peptide hydrogels for neural tissue engineering. ACS Biomaterials Science and Engineering, 1(6), pp. 431-439. (doi: 10.1021/acsbiomaterials.5b00051) (PMID:26240838) (PMCID:PMC4517957)

Bishop, P., Rubin, P., Thomson, A. R. , Rocca, D. and Henley, J. M. (2014) The ubiquitin C-terminal hydrolase L1 (UCH-L1) C terminus plays a key role in protein stability, but its farnesylation is not required for membrane association in primary neurons. Journal of Biological Chemistry, 289(52), pp. 36140-36149. (doi: 10.1074/jbc.M114.557124) (PMID:25326379) (PMCID:PMC4276877)

Wood, C. W., Bruning, M., Ibarra, A. Á., Bartlett, G. J., Thomson, A. R. , Sessions, R. B., Brady, R. L. and Woolfson, D. N. (2014) CCBuilder: an interactive web-based tool for building, designing and assessing coiled-coil protein assemblies. Bioinformatics, 30(21), pp. 3029-3035. (doi: 10.1093/bioinformatics/btu502) (PMID:25064570) (PMCID:PMC4201159)

Thomson, A. R. , Wood, C. W., Burton, A. J., Bartlett, G. J., Sessions, R. B., Brady, R. L. and Woolfson, D. N. (2014) Computational design of water-soluble α-helical barrels. Science, 346(6208), pp. 485-488. (doi: 10.1126/science.1257452) (PMID:25342807)

Mehrban, N., Abelardo, E., Wasmuth, A., Hudson, K. L., Mullen, L. M., Thomson, A. R. , Birchall, M. A. and Woolfson, D. N. (2014) Assessing cellular response to functionalized α-helical peptide hydrogels. Advanced Healthcare Materials, 3(9), pp. 1387-1391. (doi: 10.1002/adhm.201400065) (PMID:24659615) (PMCID:PMC4276410)

Sharp, T. H., Bruning, M., Mantell, J., Sessions, R. B., Thomson, A. R. , Zaccai, N. R., Brady, R. L., Verkade, P. and Woolfson, D. N. (2012) Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design. Proceedings of the National Academy of Sciences of the United States of America, 109(33), pp. 13266-13271. (doi: 10.1073/pnas.1118622109) (PMID:22847414) (PMCID:PMC3421226)

Woolfson, D. N., Bartlett, G. J., Bruning, M. and Thomson, A. R. (2012) New currency for old rope: from coiled-coil assemblies to α-helical barrels. Current Opinion in Structural Biology, 22(4), pp. 432-441. (doi: 10.1016/j.sbi.2012.03.002) (PMID:22445228)

Zaccai, N. R. et al. (2011) A de novo peptide hexamer with a mutable channel. Nature Chemical Biology, 7(12), pp. 935-941. (doi: 10.1038/nchembio.692) (PMID:22037471) (PMCID:PMC3223406)

Mahmoud, Z. N., Gunnoo, S. B., Thomson, A. R. , Fletcher, J. M. and Woolfson, D. N. (2011) Bioorthogonal dual functionalization of self-assembling peptide fibers. Biomaterials, 32(15), pp. 3712-3720. (doi: 10.1016/j.biomaterials.2010.12.002) (PMID:21353303)

Stephanou, A. S., Roberts, G. A., Cooper, L. P., Clarke, D. J., Thomson, A. R. , MacKay, C. L., Nutley, M., Cooper, A. and Dryden, D. T.F. (2009) Dissection of the DNA mimicry of the bacteriophage T7 Ocr protein using chemical modification. Journal of Molecular Biology, 391(3), pp. 565-576. (doi: 10.1016/j.jmb.2009.06.020) (PMID:19523474) (PMCID:PMC2806950)

Armstrong, C. T., Boyle, A. L., Bromley, E. H.C., Mahmoud, Z. N., Smith, L., Thomson, A. R. and Woolfson, D. N. (2009) Rational design of peptide-based building blocks for nanoscience and synthetic biology. Faraday Discussions, 143, pp. 305-317. (doi: 10.1039/B901610D) (PMID:20334109)

Leigh, D. A., Lusby, P. J., McBurney, R. T., Morelli, A., Slawin, A. M.Z., Thomson, A. R. and Walker, D. B. (2009) Getting harder: cobalt (III)-template synthesis of catenanes and rotaxanes. Journal of the American Chemical Society, 131(10), pp. 3762-3771. (doi: 10.1021/ja809627j) (PMID:19275264)

Bromley, E. H.C., Sessions, R. B., Thomson, A. R. and Woolfson, D. N. (2009) Designed α-helical tectons for constructing multicomponent synthetic biological systems. Journal of the American Chemical Society, 131(3), pp. 928-930. (doi: 10.1021/ja804231a) (PMID:19115943)

Leigh, D. A. and Thomson, A. R. (2008) An ammonium/bis-ammonium switchable molecular shuttle. Tetrahedron Letters, 64(36), pp. 8411-8416. (doi: 10.1016/j.tet.2008.05.130)

Dryden, D. T.F., Thomson, A. R. and White, J. H. (2008) How much of protein sequence space has been explored by life on Earth? Journal of the Royal Society: Interface, 5(25), pp. 953-956. (doi: 10.1098/rsif.2008.0085) (PMID:18426772) (PMCID:PMC2459213)

Leigh, D. A. and Thomson, A. R. (2006) Switchable dual binding mode molecular shuttle. Organic Letters, 8(23), pp. 5377-5379. (doi: 10.1021/ol062284j) (PMID:17078722)

Aucagne, V., Leigh, D. A., Lock, J. S. and Thomson, A. R. (2006) Rotaxanes of cyclic peptides. Journal of the American Chemical Society, 128(6), pp. 1784-1785. (doi: 10.1021/ja057206q) (PMID:16464065)

This list was generated on Fri Jul 30 21:11:44 2021 BST.

Grants

We have funding through EPSRC grants and via the Leverhulme Trust.

Supervision

PhD Students

Selma Crecente Garcia

PhD Student 2017-2021

Selma works on the design of beta turn mimics and peptides that exhibit conformational switching behaviour. Selma has skills in peptide synthesis, peptide/protein NMR, and peptide biophysics.

Bethany Atkinson

PhD Student 2018-2022

Bethany works on the conformational design of cyclic peptides, as well as peptide ligation methods. Bethany is an expert in enhanced sampling molecular dynamics methods, as well as peptide synthesis and biophysical analysis.

Pernille Christensen

PhD Student 2020 -2023

Pernille is working on methods for generating mimics of helical proteins through chemical ligation reactions. This involves a mix of organic synthesis, peptide chemistry, and protein biophysics methods.

Robbie Stirling

PhD Student 2021-2024

Robbie will be joining in October 2021 for an EPSRC funded studentship that will explore adding different chemical functions to our chemical ligation methods to make new probe molecules for chemical biology.

Cameron McAnespie

PhD Student 2021-2024

Cameron will be joining in October 2021 through the LifETIME CDT, and will be working on hybrid peptide/polymer materials for tissue engineering applications.

Danielle Liebnitz

PhD Student 2021-2024

Danielle will join us for a Leverhulme Trust funded studentship starting Oct 2021, joint with the group of Prof Ross Forgan. The project will involve making new and interesting chiral peptide/inorganic hybrid structures.

Postdoctoral Researchers

Beckie Clarke

PDRA 2019-2023

Beckie works jointly with the group of Prof Andy Sutherland on the synthesis of fluorescent amino acids and their incorporation into designed peptides/proteins. These will form the basis of new chiroptical sensing methods. This is part of an EPSRC funded project led by Prof Malcolm Kadodwala

Teaching

Level 1: Organic Chemistry 2

Level 3: Organic Synthesis 1

Chemical Biology PGT: Joint Course Coordinator and Bioconjugation Lecture course.