Dr Aneika Leney PhD

School of Biosciences
Associate Professor of Biological Mass Spectrometry

Contact details

Address
School of Biosciences
University of Birmingham
Edgbaston
Birmingham
B15 2TT
UK

Dr Leney is a structural biology-based mass spectrometrist. Her interests focus on protein post-translational modifications and the role that these play in communication or miscommunication in the case of disease. She is also exploring new avenues whereby protein modifications can be utilised for biotechnological applications.

More information: https://www.leney-mass-spectrometry.com/

Qualifications

PhD (2013) University of Leeds

BSc (2008) in Biochemistry with a Year in Industry, University of York

Biography

Aneika Leney graduated from the University of York in 2008. During her degree, she undertook an industrial placement at GlaxoSmithKline which fueled her interest to pursue a career in Mass Spectrometry. For her PhD, she joined the Astbury Centre at the University Leeds whereby she was supervised by Professors Sheena Radford and Alison Aschroft on projects that utilised mass spectrometry to study protein structure and function.

Following her scientific interests, Aneika moved to Canada and joined the Alberta Glycomics Centre. Her post-doctoral research there involved the development of novel methodology to monitor protein-ligand interactions. Subsequent to this, she moved to a world-leading laboratory at Utrecht University in the Netherlands, whereby she performed outstanding proteomics research under the supervision of Professor Albert Heck. Her work focussing on protein post-translational modifications and how these alter protein function.

At the University of Birmingham, Aneika leads her own research group focusing on protein structure and function. Her group utilises state-of-the-art mass spectrometry techniques to analyse proteins and protein complexes. Her research aimed at tackling the biological question of how proteins communicate and switch between their active and inactive states. Aneika’s research also explores how protein modifications can be used in biotechnological applications such as in food colouring, protein visualisation and for harvesting light energy for use in solar panels.

Teaching

Aneika teaches predominantly of the Biochemistry course to all year groups. Aneika enjoys leading a variety of biochemical projects for undergraduate and masters’ students.

Postgraduate supervision

Research projects in the Leney Lab focus in two areas:

1) The use of mass spectrometry to monitor post-translational modifications involved in health and disease

2) The characterization and identification of post-translation modification in large biological complexes for use in biotechnological applications 

Please also refer to:

www.findaphd.com page here

Please contact Aneika Leney regarding the latest projects on offer. We welcome students with a strong biochemistry background/with mass spectrometry experience.

Research

Research Theme within School of Biosciences: Cells and Molecules and Plant Science.

Researcher identifier number: https://orcid.org/0000-0002-2066-4950

Structural biology-based Mass Spectrometry

leney-research-imageThe Leney lab is interested in utilising state-of-the-art mass spectrometers to analyse proteins and protein complexes. Our research focuses on protein post-translational modifications and how they modulate protein function. Protein modifications can be detrimental to human health, for example hyper-phosphorylated proteins can be found in Alzheimer’s disease patients. However, protein modifications can also have interesting biotechnological applications, such as in dyes for use in the food and cosmetics industry. 

Our research combines both development of novel techniques to analyse protein post-translational modifications and their application to solve complex biological problems.

More information: https://www.leney-mass-spectrometry.com/

Publications

Recent publications

Article

Adoni, KR, Cunningham, DL, Heath, JK & Leney, AC 2022, 'FAIMS enhances the detection of PTM crosstalk sites', Journal of Proteome Research, vol. 21, no. 4, pp. 930-939. https://doi.org/10.1021/acs.jproteome.1c00721

Bellamy-Carter, J, Sound, JK & Leney, AC 2022, 'Probing heavy metal binding to phycobiliproteins', The FEBS journal. https://doi.org/10.1111/febs.16396

Bellamy-Carter, J, Mohata, M, Falcicchio, M, Basran, J, Higuchi, Y, Doveston, RG & Leney, AC 2021, 'Discovering protein–protein interaction stabilisers by native mass spectrometry', Chemical Science. https://doi.org/10.1039/D1SC01450A

Sound, JK, Peters, A, Bellamy-Carter, J, Rad-Menéndez, C, MacKechnie, K, Green, DH & Leney, AC 2021, 'Rapid cyanobacteria species identification with high sensitivity using native mass spectrometry', Analytical Chemistry, vol. 93, no. 42, pp. 14293-14299. https://doi.org/10.1021/acs.analchem.1c03412

Tamara, S, Hoek, M, Scheltema, RA, Leney, AC & Heck, AJR 2019, 'A Colorful Pallet of B-Phycoerythrin Proteoforms Exposed by a Multimodal Mass Spectrometry Approach', Chem, vol. 5, no. 5, pp. 1302-1317. https://doi.org/10.1016/j.chempr.2019.03.006

Hughes, G, Hall, S, Laxton, C, Sridhar, P, Mahadi, A, Hatton, C, Piggot, T, Wotherspoon, P, Leney, A, Ward, D, Jamshad, M, Spana, V, Cadby, I, Harding, C, Isom, G, Bryant, J, Parr, R, Yakub, Y, Jeeves, M, Huber, D, Henderson, I, Clifton, L, Lovering, A & Knowles, T 2019, 'Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system', Nature Microbiology, vol. 4, no. 10, pp. 1692–1705. https://doi.org/10.1038/s41564-019-0481-y

Muha, V, Williamson, R, Hills, R, McNeilly, AD, McWilliams, TG, Alonso, J, Schimpl, M, Leney, AC, Heck, AJR, Sutherland, C, Read, KD, McCrimmon, RJ, Brooks, SP & Van Aalten, DMF 2019, 'Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice', Open Biology, vol. 9, no. 11, 190192, pp. 1-15. https://doi.org/10.1098/rsob.190192

Leney, AC 2019, 'Subunit pI Can Influence Protein Complex Dissociation Characteristics', Journal of the American Society for Mass Spectrometry. https://doi.org/10.1007/s13361-019-02198-3

Leney, AC, Tschanz, A & Heck, AJR 2018, 'Connecting color with assembly in the fluorescent B-phycoerythrin protein complex', FEBS Journal, vol. 285, no. 1, pp. 178-187. https://doi.org/10.1111/febs.14331

Leney, AC, Rafie, K, Van Aalten, DMF & Heck, AJR 2017, 'Direct Monitoring of Protein O-GlcNAcylation by High-Resolution Native Mass Spectrometry', ACS chemical biology, vol. 12, no. 8, pp. 2078-2084. https://doi.org/10.1021/acschembio.7b00371

Leney, AC, El Atmioui, D, Wu, W, Ovaa, H & Heck, AJR 2017, 'Elucidating crosstalk mechanisms between phosphorylation and O-GlcNAcylation', Proceedings of the National Academy of Sciences of the United States of America, vol. 114, no. 35, pp. E7255-E7261. https://doi.org/10.1073/pnas.1620529114

Tamara, S, Scheltema, RA, Heck, AJR & Leney, AC 2017, 'Phosphate Transfer in Activated Protein Complexes Reveals Interaction Sites', Angewandte Chemie - International Edition, vol. 56, no. 44, pp. 13641-13644. https://doi.org/10.1002/anie.201706749

Editorial

Cooper, HJ & Leney, AC 2021, 'Structural proteomics and protein complexes – special issue', Proteomics, vol. 21, no. 21-22, 2000286. https://doi.org/10.1002/pmic.202000286

Review article

van der Laarse, SAM, Leney, AC & Heck, AJR 2018, 'Crosstalk between phosphorylation and O-GlcNAcylation: friend or foe', FEBS Journal, vol. 285, no. 17, pp. 3152-3167. https://doi.org/10.1111/febs.14491

Leney, AC & Heck, AJR 2017, 'Native mass spectrometry: what is in the name?', Journal of the American Society for Mass Spectrometry, vol. 28, no. 1, pp. 5-13. https://doi.org/10.1007/s13361-016-1545-3

View all publications in research portal