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Dr Guto Rhys
(he/him)
Lecturer in Biological Chemistry
- Welsh speaking
- Available for postgraduate supervision
Overview
The Rhys lab is interested in designing new, and engineering existing, peptides and proteins. The latest developments in experimental methods and computational algorithms enable us to develop new peptides and proteins that do not exist in nature. We are developing a team of highly interdisciplinary scientists to tackle some of the unmet challenges that society faces. These include developing new therapeutics for diseases that are currently difficult to treat, and new enzymes to replace chemical reactions that are bad for the environment.
Our lab is always open to new collaborations. Our lab is also a supportive environment that cares about the development of its students and staff. We welcome anyone regardless of age, disability, ethnicity, gender and sexual orientation. We are open to anyone looking to contribute to making the lab a diverse, inclusive and friendly environment.
For up-to-date information please visit www.rhyslab.com
Publication
2023
- Dawson, W. M. et al. 2023. Differential sensing with arrays of de novo designed peptide assemblies. Nature Communications 14, article number: 383. (10.1038/s41467-023-36024-y)
2022
- Rhys, G. G. et al. 2022. De novo designed peptides for cellular delivery and subcellular localisation. Nature Chemical Biology 18(9), pp. 999-1004. (10.1038/s41589-022-01076-6)
2021
- Dawson, W. M. et al. 2021. Structural resolution of switchable states of a de novo peptide assembly. Nature Communications 12(1), article number: 1530. (10.1038/s41467-021-21851-8)
- 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) (10.1021/acs.biomac.1c00131)
- Dawson, W. M., Martin, F. J. O., Rhys, G. G., Shelley, K. L., Brady, R. L. and Woolfson, D. N. 2021. Coiled coils 9-to-5: rational de novo design of α-helical barrels with tunable oligomeric states. Chemical Science 12(20), pp. 6923-6928. (10.1039/D1SC00460C)
2019
- Dawson, W. M., Rhys, G. G. and Woolfson, D. N. 2019. Towards functional de novo designed proteins. Current Opinion in Chemical Biology 52, pp. 102-111. (10.1016/j.cbpa.2019.06.011)
- Boyle, A. L. et al. 2019. Selective coordination of three transition metal ions within a coiled-coil peptide scaffold. Chemical Science 10(31), pp. 7456-7465. (10.1039/C9SC01165J)
- Rhys, G. G. et al. 2019. Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society 141(22), pp. 8787-8797. (10.1021/jacs.8b13354)
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), article number: 4132. (10.1038/s41467-018-06391-y)
- Fletcher, J. M., Horner, K. A., Bartlett, G. J., Rhys, G. G., Wilson, A. J. and Woolfson, D. N. 2018. De novocoiled-coil peptides as scaffolds for disrupting protein–protein interactions. Chemical Science 9(39), pp. 7656-7665. (10.1039/C8SC02643B)
- Thomas, F. et al. 2018. De novo-designed α-helical barrels as receptors for small molecules. ACS Synthetic Biology 7(7), pp. 1808-1816. (10.1021/acssynbio.8b00225)
- Galloway, J. M. et al. 2018. Bioinspired silicification reveals structural detail in self-assembled peptide cages. ACS Nano 12(2), pp. 1420-1432. (10.1021/acsnano.7b07785)
Articles
- Dawson, W. M. et al. 2023. Differential sensing with arrays of de novo designed peptide assemblies. Nature Communications 14, article number: 383. (10.1038/s41467-023-36024-y)
- Rhys, G. G. et al. 2022. De novo designed peptides for cellular delivery and subcellular localisation. Nature Chemical Biology 18(9), pp. 999-1004. (10.1038/s41589-022-01076-6)
- Dawson, W. M. et al. 2021. Structural resolution of switchable states of a de novo peptide assembly. Nature Communications 12(1), article number: 1530. (10.1038/s41467-021-21851-8)
- 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) (10.1021/acs.biomac.1c00131)
- Dawson, W. M., Martin, F. J. O., Rhys, G. G., Shelley, K. L., Brady, R. L. and Woolfson, D. N. 2021. Coiled coils 9-to-5: rational de novo design of α-helical barrels with tunable oligomeric states. Chemical Science 12(20), pp. 6923-6928. (10.1039/D1SC00460C)
- Dawson, W. M., Rhys, G. G. and Woolfson, D. N. 2019. Towards functional de novo designed proteins. Current Opinion in Chemical Biology 52, pp. 102-111. (10.1016/j.cbpa.2019.06.011)
- Boyle, A. L. et al. 2019. Selective coordination of three transition metal ions within a coiled-coil peptide scaffold. Chemical Science 10(31), pp. 7456-7465. (10.1039/C9SC01165J)
- Rhys, G. G. et al. 2019. Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society 141(22), pp. 8787-8797. (10.1021/jacs.8b13354)
- 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), article number: 4132. (10.1038/s41467-018-06391-y)
- Fletcher, J. M., Horner, K. A., Bartlett, G. J., Rhys, G. G., Wilson, A. J. and Woolfson, D. N. 2018. De novocoiled-coil peptides as scaffolds for disrupting protein–protein interactions. Chemical Science 9(39), pp. 7656-7665. (10.1039/C8SC02643B)
- Thomas, F. et al. 2018. De novo-designed α-helical barrels as receptors for small molecules. ACS Synthetic Biology 7(7), pp. 1808-1816. (10.1021/acssynbio.8b00225)
- Galloway, J. M. et al. 2018. Bioinspired silicification reveals structural detail in self-assembled peptide cages. ACS Nano 12(2), pp. 1420-1432. (10.1021/acsnano.7b07785)
Research
New-to-nature biocatalysis
Since the beginning of the research group in 2023, our main research area is within biocatalysis, where we wish to design and engineer enzymes that can catalyse chemical reactions that are rarely or never observed in nature. To achieve this, we are developing artificial metalloenzymes, which are proteins that contain non-natural metals or metal-containing cofactors. These abiological cofactors can catalyse new-to-nature chemical transformations. We expect that we can go beyond what is achievable with organic chemistry or natural enzymes alone, to deliver a sustainable route to the production of fine chemicals based on renewable feedstocks.
Currently active grant
EPSRC New Investigator Award Stereoselective synthesis of biaryl compounds catalysed by artificial metalloenzymes
Teaching
Module lead
CH5110 Year 1 Chemistry Foundation Practical
Contributor
CH4305 Macromolecules of life
Supervisions
In the Rhys lab we train people to have a highly diverse skillset, which will make them highly employable when taking the next step in their career. Skills that members of the team routinely employ include:
- Recombinant protein expression
- Computational protein design
- Organic synthesis
- Biocatalysis
- Green chemistry
- Structural biology
- Enzyme engineering
- High-throughput screening using robotics
- Programming
Current supervision
Benjamin Orton
Graduate Demonstrator
Research themes
Specialisms
- Protein design and engineering
- Proteins and peptides
- Organic chemistry
- Bioinformatics and computational biology
- Environmental biotechnology