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

Import to contacts

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.

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

We do a mix of peptide synthesis, protein design, and supramolecular organic chemistry. If we can get all of these components to work well together then we end up doing some fun and interesting science that addresses funamental questions about how peptides and proteins interact with each other, and how we can design new peptides. 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:

Coiled coil binders of proteins

A recent focus in our lab has been on the design/engineering of peptides that bind protein targets. We have recently shown that we can engineer small, super-stable coiled coil structures to mimic known peptide-protein interactions, with increased binding affinity. In collaboration with the lab of Prof Danny Huang, we have developed binders of the protein Ubiquitin, as well as for other biologically and medically important proteins.

 

We are at the moment expanding this method to other targets. If you think this might work for your protein target drop us a line!

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, including for the alpha-helical systems described above). We have also shown that we can use these methods to generate cyclic peptides with controlled conformation.

Peptides in Supramolecular Chemistry

We are currently exploring the interaction of coiled coil peptides with supramolecular systems such as metal-ligand binding. In particular, we are interested in the interplay between peptide supercoiling and chirality of a connected transition metal complex. Learning about the interaction between these two types of chirality allows us to examine how chiral information is transferred in complex molecules.

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. We are also working with the Adams Group in Glasgow to design new peptide biomaterials.

Research groups

Publications

List by: Type | Date

Jump to: 2024 | 2022 | 2021 | 2020 | 2019 | 2018 | 2017 | 2016 | 2015 | 2014 | 2012 | 2011 | 2009 | 2008 | 2006
Number of items: 36.

2024

Clarke, R. , Zeng, L., Atkinson, B. C., Kadodwala, M. , Thomson, A. R. and Sutherland, A. (2024) Fluorescent carbazole-derived α-amino acids; structural mimics of tryptophan. Chemical Science, 15(16), pp. 5944-5949. (doi: 10.1039/D4SC01173B) (PMID:38665535) (PMCID:PMC11040653)

2022

Tabouillot, V. et al. (2022) Near-field probing of optical superchirality with plasmonic circularly polarized luminescence for enhanced bio-detection. ACS Photonics, 9(11), pp. 3617-3624. (doi: 10.1021/acsphotonics.2c01073) (PMID:36411820)

Atkinson, B. C. and Thomson, A. R. (2022) Structured cyclic peptide mimics by chemical ligation. Peptide Science, 114(5), e24266. (doi: 10.1002/pep2.24266)

2021

Scott, A. J. et al. (2021) Constructing ion channels from water-soluble α-helical barrels. Nature Chemistry, 13(7), pp. 643-650. (doi: 10.1038/s41557-021-00688-0) (PMID:33972753) (PMCID:PMC7611114)

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, 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 Sun Jul 21 20:31:35 2024 BST.
Jump to: Articles
Number of items: 36.

Articles

Clarke, R. , Zeng, L., Atkinson, B. C., Kadodwala, M. , Thomson, A. R. and Sutherland, A. (2024) Fluorescent carbazole-derived α-amino acids; structural mimics of tryptophan. Chemical Science, 15(16), pp. 5944-5949. (doi: 10.1039/D4SC01173B) (PMID:38665535) (PMCID:PMC11040653)

Tabouillot, V. et al. (2022) Near-field probing of optical superchirality with plasmonic circularly polarized luminescence for enhanced bio-detection. ACS Photonics, 9(11), pp. 3617-3624. (doi: 10.1021/acsphotonics.2c01073) (PMID:36411820)

Atkinson, B. C. and Thomson, A. R. (2022) Structured cyclic peptide mimics by chemical ligation. Peptide Science, 114(5), e24266. (doi: 10.1002/pep2.24266)

Scott, A. J. et al. (2021) Constructing ion channels from water-soluble α-helical barrels. Nature Chemistry, 13(7), pp. 643-650. (doi: 10.1038/s41557-021-00688-0) (PMID:33972753) (PMCID:PMC7611114)

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, 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 Sun Jul 21 20:31:35 2024 BST.

Grants

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

Supervision

Current Group Members

Danielle Liebnitz

PhD Student 2021-2025

Danielle is supported by a Leverhulme Trust funded studentship, joint with the group of Prof Ross Forgan. Her project will involves making new and interesting chiral peptide/inorganic hybrid structures. This project is funded by the Leverhulme Trust.

 

Adelaide Lunga

PhD Student 2023-2027

Adelaide is working on the design of peptides that bind the protein ubiquitin, with a view to the selective detection of different ubiquitin chain linkages. This project is funded through the James McCune Smith programme, supported by GSK.

 

Athena Mattheou

PhD Student 2023-2027

Athena is working on the design and synthesis of peptide-polymer hybrid materials as novel scaffolds for cell engineering applications. This project is funded through the LifETIME CDT.

 

Group Alumni

Pernille Christensen

PhD Student 2020 -2024

Pernille worked on the design and synthesis of helical mimics of known peptide:protein interactions.

 

Beckie Clarke

PDRA 2019-2023

Beckie worked jointly with the group of Prof Andy Sutherland on the synthesis of fluorescent amino acids and their incorporation into designed peptides/proteins

 

Bethany Atkinson

PhD Student 2018-2022

Bethany worked on the conformational design of cyclic peptides, as well as peptide ligation methods.

 

Selma Crecente Garcia

PhD Student 2017-2021

Selma worked on the design of beta turn mimics and peptides that exhibit conformational switching behaviour.

Teaching

Level 1: Organic Chemistry 2

Level 3: Organic Synthesis 1

Chemical Biology PGT: Bioconjugation Chemistry