My research concerns protein self-assembly related to neurodegenerative diseases with the focus on characterization of protein structure and molecular mechanisms of self-assembly. The studies in our lab include a broad range of different techniques within biophysics, protein biochemistry and biomedicine. My current research focuses on the aggregation mechanisms of amyloid-β peptide (Aβ) fibril formation, associated to Alzheimer’s disease and inhibition mechanisms by the BRICHOS domain, a chaperone-like protein that is potential candidate to be implemented in Alzheimer’s disease treatment. Furthermore, another research line is the development of new expression and purification protocols for aggregation-prone proteins using a spider silk-derived solubility tag, where one possible application is the generation of new biomaterials.
Please visit our group homepage for more information:
Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state. Chen G#, Abelein A#, Nilsson HE, Leppert A, Andrade-Talavera Y, Tambaro S, et al Nat Commun 2017 12;8(1):2081; # equal contributions
Zinc as chaperone-mimicking agent for retardation of amyloid β peptide fibril formation. Abelein A, Gräslund A, Danielsson J Proc Natl Acad Sci U S A 2015 Apr;112(17):5407-12
Ionic Strength Modulation of the Free Energy Landscape of Aβ40 Peptide Fibril Formation. Abelein A, Jarvet J, Barth A, Gräslund A, Danielsson J J Am Chem Soc 2016 06;138(21):6893-902
High-yield Production of Amyloid-β Peptide Enabled by a Customized Spider Silk Domain. Abelein A, Chen G, Kitoka K, Aleksis R, Oleskovs F, Sarr M, et al Sci Rep 2020 01;10(1):235
Metal ion coordination delays amyloid-β peptide self-assembly by forming an aggregation-inert complex. Wallin C, Jarvet J, Biverstål H, Wärmländer S, Danielsson J, Gräslund A, Abelein A J Biol Chem 2020 May;295(21):7224-7234