Dr Alexandra Males BSc, MRSC, AFHEA, PhD

Lecturer in Analytical Chemistry

Summary

I was appointed as a lecturer at Sheffield Hallam University in 2023. My teaching responsibilities involve analytical chemistry topics for example, separations, calibrations, spectroscopy and others. I am interested in glycobiology research using the mass spectrometry imaging suite.

About

After completing a BSc in Biochemistry at The University of Sheffield, I worked at the Oxford Protein Production Facility in the Research Complex at Harwell. I was involved in crystallising proteins from difficult projects.

After this, I completed my PhD in 2019 at the University of York under the guidance of Professor Gideon Davies. My thesis is titled 'structure and function of glycoside hydrolase enzymes involved in mannose and N-acetylglucosamine processing'. My research involved characterising carbohydrate enzymes through structural biology techniques (x-ray crystallography) and analysis of substrates by mass spectrometry. During this time, I was awarded the Kathleen Mary Stott award for recognition of scientific excellence. Within the same group, I took a position as a postdoctoral researcher to continue the work from my PhD.

In 2022, I became an associate lecturer in the Department of Chemistry at the University of York. I was responsible for teaching enzyme kinetics lectures, tutorials, workshops and laboratory classes to chemistry, biochemistry and natural science students.

Teaching

School of Biosciences and Chemistry

College of Health, Wellbeing and Life Sciences

Module leader for Innovations and analytical science module, MSc Analytical Chemistry.

Courses taught:
- BSc Chemistry,
- BSc Biochemistry,
- BSc BMS, MSc Analytical Chemistry

Modules taught:
- Analytical and bioanalytical science
- Frontiers of chemical research
- Innovations in analytical science
- Principles of chemistry and analytical science
- Surface analysis and related techniques
- Laboratory classes across all levels

Research

Analysing the effects of carbohydrates involved in medical diseases.

Further information to come.

Publications

Journal articles

Males, A., Kok, K., Nin-Hill, A., de Koster, N., van den Beukel, S., Beenakker, T.J.M., ... Artola, M. (2023). Trans-cyclosulfamidate mannose-configured cyclitol allows isoform-dependent inhibition of GH47 α-d-mannosidases through a bump–hole strategy. Chemical Science. http://doi.org/10.1039/d3sc05016e

Calvelo, M., Males, A., Alteen, M.G., Willems, L.I., Vocadlo, D.J., Davies, G.J., & Rovira, C. (2023). Human O-GlcNAcase Uses a Preactivated Boat-skew Substrate Conformation for Catalysis. Evidence from X-ray Crystallography and QM/MM Metadynamics. ACS Catalysis, 13 (20), 13672-13678. http://doi.org/10.1021/acscatal.3c02378

Burchill, L., Males, A., Kaur, A., Davies, G.J., & Williams, S.J. (2022). Structure, Function and Mechanism of N‐Glycan Processing Enzymes: endo‐α‐1,2‐Mannanase and endo‐α‐1,2‐Mannosidase. Israel Journal of Chemistry, 63 (1-2). http://doi.org/10.1002/ijch.202200067

González-Cuesta, M., Sidhu, P., Ashmus, R.A., Males, A., Proceviat, C., Madden, Z., ... Vocadlo, D.J. (2022). Bicyclic Picomolar OGA Inhibitors Enable Chemoproteomic Mapping of Its Endogenous Post-translational Modifications. Journal of the American Chemical Society, 144 (2), 832-844. http://doi.org/10.1021/jacs.1c10504

Schröder, S.P., Offen, W.A., Males, A., Jin, Y., Enotarpi, J., de Boer, C., ... Davies, G.J. (2021). Development of Non-Hydrolysable Oligosaccharide Activity-Based Inactivators for Endoglycanases: A Case Study on α-1,6 Mannanases. Chemistry - A European Journal, 27 (37), 9519-9523. http://doi.org/10.1002/chem.202101255

Rovira, C., Males, A., Davies, G.J., & Williams, S.J. (2020). Mannosidase mechanism: at the intersection of conformation and catalysis. Current opinion in structural biology, 62, 79-92. http://doi.org/10.1016/j.sbi.2019.11.008

King, D.T., Males, A., Davies, G.J., & Vocadlo, D.J. (2019). Molecular mechanisms regulating O-linked N-acetylglucosamine (O-GlcNAc)-processing enzymes. Current opinion in chemical biology, 53, 131-144. http://doi.org/10.1016/j.cbpa.2019.09.001

Sernee, M.F., Ralton, J.E., Nero, T.L., Sobala, L.F., Kloehn, J., Vieira-Lara, M.A., ... McConville, M.J. (2019). A Family of Dual-Activity Glycosyltransferase-Phosphorylases Mediates Mannogen Turnover and Virulence in Leishmania Parasites. Cell host & microbe, 26 (3), 385-399.e9. http://doi.org/10.1016/j.chom.2019.08.009

Males, A., Speciale, G., Williams, S.J., & Davies, G.J. (2019). Distortion of mannoimidazole supports a B_2,5 boat transition state for the family GH125 α-1,6-mannosidase from Clostridium perfringens. Organic & biomolecular chemistry, 17 (34), 7863-7869. http://doi.org/10.1039/c9ob01161g

Males, A., & Davies, G.J. (2019). Structural studies of a surface-entropy reduction mutant of O-GlcNAcase. Acta crystallographica. Section D, Structural biology, 75 (Pt 1), 70-78. http://doi.org/10.1107/s2059798318016595

Males, A., Raich, L., Williams, S.J., Rovira, C., & Davies, G.J. (2017). Conformational Analysis of the Mannosidase Inhibitor Kifunensine: A Quantum Mechanical and Structural Approach. Chembiochem : a European journal of chemical biology, 18 (15), 1496-1501. http://doi.org/10.1002/cbic.201700166

van Rijssel, E.R., Janssen, A.P.A., Males, A., Davies, G.J., van der Marel, G.A., Overkleeft, H.S., & Codée, J.D.C. (2017). Conformational Behaviour of Azasugars Based on Mannuronic Acid. Chembiochem : a European journal of chemical biology, 18 (13), 1297-1304. http://doi.org/10.1002/cbic.201700080

Alonso-Gil, S., Males, A., Fernandes, P.Z., Williams, S.J., Davies, G.J., & Rovira, C. (2017). Computational Design of Experiment Unveils the Conformational Reaction Coordinate of GH125 α-Mannosidases. Journal of the American Chemical Society, 139 (3), 1085-1088. http://doi.org/10.1021/jacs.6b11247

Ren, J., Nettleship, J.E., Males, A., Stuart, D.I., & Owens, R.J. (2016). Crystal structures of penicillin-binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms. FEBS letters, 590 (2), 288-297. http://doi.org/10.1002/1873-3468.12054

Alexandra Males