Dr Aneika Leney PhD

Dr Aneika Leney

School of Biosciences
Lecturer in Biological Mass Spectrometry

Contact details

School of Biosciences
University of Birmingham
B15 2TT

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/


PhD (2013) University of Leeds

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


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.


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 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/


Muha V., Williamson R., Hills R., McNeilly A.D., McWilliams T.G., Alonso, J., Schimpl M., Leney A.C., Heck A.J.R., Sutherland C., Read K.D., McCrimmon R.J., Brooks S.P., van Aalten D.M.F.. Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice. Open biology (2019) 9 (11), 190192.

Hughes G.W., Hall S.C.L., Laxton C.S., Sridhar P., Mahadi A.H., Hatton C., Piggot T.J., Wotherspoon P.J., Leney A.C., Ward D.G., Jamshad M., Spana V., Cadby I.T., Harding C., Isom G.L., Bryant J.A., Parr R.J., Yakub Y., Jeeves M., Huber D., Henderson I.R., Clifton L.A., Lovering A.L., Knowles T.J. Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system. Nat. microbiol. (2019) 4 (10), 1692-1705. 

Leney A.C. Subunit pI can influence protein complex dissociation characteristics. J. Am. Soc. Mass Spectrom. (2019) 30 (8), 1389-1395.

Tamara S., Hoek M., Scheltema R.A., Leney A.C., Heck A.J.R.. A colorful pallet of B-phycoerythrin proteoforms exposed by a multimodal mass spectrometry approach. Chem. (2019) 5 (5), 1302-1317.

Laarse S.A.M+, Leney A.C.+, Heck A.J.R. Crosstalk between phosphorylation and O-GlcNAcylation: friend or foe. FEBS J. (2018) DOI: 10.1111/febs.14491.

Leney A.C.*, Tschanz A., Heck A.J.R. Connecting color with assembly in the fluorescent B-phycoerythrin protein complex. FEBS J. (2018) 285(1): 178-187.

Tamara S., Scheltema R.A., Heck A.J.R.*, Leney A.C.* Phosphate transfer in activated protein complexes reveal interaction sites. Angew. Chem. (2017) 129(44): 13829-13832.

Leney A.C., Atmioui D.E., Wu W., Ovaa H., Heck A.J.R. Elucidating cross-talk mechanisms between phosphorylation and O-GlcNAcylation. Prot. Nat. Acad. Sci. (2017) 114(35): 7255-7261.

Leney A.C., Rafie K., van Aalten D.M.F., Heck A.J.R. Direct Monitoring of protein O-GlcNAcylation by high-resolution native mass spectrometry. ACS Chem. Biol. (2017) 12(8): 2078-2084.

Leney A.C., Heck A.J.R. Native mass spectrometry: what is in the name? J. Am. Soc. Mass Spectrom. (2017) 28(1): 5-13.

Lössl P., Brunner A.M., Lui F., Leney A.C., Yamashita M., Scheltema R.A., Heck A.J.R. Deciphering the interplay among multi-site phosphorylation, interaction dynamics and conformational transitions in a tripartite protein system. ACS Cent. Sci. (2016) 2(7):445-455.

Marino F., Bern M., Mommen G.P.M., Leney A.C., Bonvin A.M.J.J., van Els C.A.C.M., Becker C., Heck A.J.R. Extended O-GlcNAc on HLA class-I-bound peptides. J. Am. Chem. Soc. (2015) 137(34):10922-10925.

Leney A.C., Darestani R.R., Li J., Nikjah S., Kitova E.N., Zou C., Cairo C.W., Xiong Z.J., Privé G.G., Klassen J.S. Picodiscs for facile protein-glycolipid analysis. Anal. Chem. (2015) 87(8):4402-4408.

Leney A.C., Xuxin F., Kitova E.N., Klassen J.S. Nanodiscs and electrospray ionization mass spectrometry: a tool for screening glycolipids against proteins. Anal. Chem. (2014) 86(11):5271-5277.

Leney A.C., Pashley C.L., Scarff C.S., Radford S.E., Ashcroft A.E. Insights into the role of the beta-2-microglobulin D-strand in amyloid propensity revealed by mass spectrometry. Mol. BioSyst. (2014) 10:412-420.

Leney A.C., McMorran, L.M., Radford, S.E., Ashcroft A.E. Amphipathic polymers enable the study of functional membrane proteins in the gas phase. Anal. Chem. (2012) 84(22):9841-9847.

Morrissey B., Leney A.C., Toste-Rego A., Allen W.J., Phan G., Waksman G., Ashcroft A.E., Radford S.E. The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS. Mol. Cell. Prot. (2012) 11:M111.015289.

* denotes corresponding author

+ denotes joint first authorship

Leney A.C., Phan G., Allen W., Verger D., Waksman G., Radford S.E., Ashcroft A.E. Second order rate constants of donor-strand exchange reveal individual amino acid residues important in determining the subunit specificity of pilus biogenesis. J. Am. Soc. Mass Spectrom. (2011) 22:1214-1223.

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