Staff Personal
Research Associate in the group of Professor Carol V. Robinson, University of Oxford and the University of Cambridge, U.K.
Nanoflow-Electrospray Mass Spectrometry of Macromolecular Complexes and Membrane Proteins.
EMBO Postdoctoral Fellow, Max Planck Institute for Biochemistry, Martinsried, GERMANY. Solution and Solid-state NMR of biomembranes and peptide-lipid interactions.
PhD, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, SWEDEN. Biochemical and Biophysical Aspects of Molecular Recognition and Signalling by Neurotrophins.
Staff Research
Nanoflow-electrospray mass spectrometry of non-covalent complexes.
Analysis of membrane proteins and macromolecular assemblies.
Staff Specialties
My research interests are on the development and application of new mass spectrometric methods to address problems in the life sciences. Focus is mainly on molecular machines and membrane proteins. Previous work in Carol Robinson’s group has been on the characterization of macromolecular complexes such as RNA polymerase, degradosome and the ribosome as well as membrane proteins like EmrE, a bacterial drug resistance pump.
In other projects we aim to investigate the environmental factors contributing to neurodegenerative diseases such as Amyotrophic lateral sclerosis (ALS), Alzheimer’s and Parkinson’s disease mindful that risk is a function of exposure and inherent toxicity of a substance. Specifically, the focus is to establish and characterise the bioincorporation of the neurotoxic amino acid b-N-methylamino-L-alanine or BMAA (and its isomers) into proteins and determine the possible mechanism(s) by which this is accomplished. This knowledge is vital for allowing the proper assessment of risk and design of possible intervention to protect populations exposed to the toxin. Our lab has made a significant contribution for detecting and identifying BMAA (Spacil, 2010) that was used to show transport of this toxin within the food chain in the Baltic Sea (Jonasson, 2010). Most recently we have elucidated how to distinguish BMAA from its isomers and quantify trace levels (Jiang, 2012/2013). We aim to determine if the incorporation is protein specific and if so identify which proteins are affected and eventually misfolded. Furthermore, we wish to continue method development to more effectively address biological issues. In this regard, by using fixed step selected reaction monitoring (FS-SRM) we plan to analyse the extent of radical damage as a function of potential disruption of superoxide dismutase (SOD) function (natural mutations of which are associated with ALS) and structure.
Spáil, Z., Eriksson, J., Jonasson, S., Rasmussen, U., Ilag, L.L., Bergman, B. (2010)
Analytical protocol for identification of BMAA and DAB in biological samples.
Analyst 135(1): 127-32.
Jonasson, S., Eriksson, J., Berntzon, L., Spacill, Z., Ilag, L.L., Ronnevi, L.
Rasmussen, U., and Bergmann, B. (2010) Transfer of a cyanobacterial neurotoxin
within a temperate aquatic ecosystem suggests pathways for human exposure
Proc Natl Acad Scie USA May 18;107(20):9252-7
Jiang, L., Aigret, B., De Borggraeve, W.; Spacil, Z.; Ilag, L.L. (2012) Selective LC
MS/MS method for the identification of BMAA from its isomers in biological
samples Anal Bioanal Chem. 403:1719–1730 .
Jiang, L., Johnston, E., Åberg, K. M., Nilsson, U. and Ilag, L. L. (2013). Strategy for
quantifying trace levels of BMAA in cyanobacteria by LC/MS/MS. Anal Bioanal
Chem 405: 1283-92.
