Thomas Näsström | lnu.se

My research groups

Physical Pharmacy Laboratory We are using chemical and physical principles to study the molecular events underlying the development and design of pharmaceutics and their formulations.

Publications

Article in journal (Refereed)

Näsström, T., Dahlberg, T., Malyshev, D., Ådén, J., Andersson, P., et al. (2021). Synthetic NAC 71-82 Peptides Designed to Produce Fibrils with Different Protofilament Interface Contacts. International Journal of Molecular Sciences. 22 (17).
Status: Published
Näsström, T., Ådén, J., Shibata, F., Andersson, P., Karlsson, B.C.G. (2020). A Capped Peptide of the Aggregation Prone NAC 71–82 Amino Acid Stretch of α-Synuclein Folds into Soluble β-Sheet Oligomers at Low and Elevated Peptide Concentrations. International Journal of Molecular Sciences. 21 (5). 1-14.
Status: Published
Näsström, T., Andersson, P., Lejon, C., Karlsson, B.C.G. (2019). Amyloid fibrils prepared using an acetylated and methyl amidated peptide model of the alpha-Synuclein NAC 71-82 amino acid stretch contain an additional cross-beta structure also found in prion proteins. Scientific Reports. 9. 1-14.
Status: Published
Fagerqvist, T., Lindström, V., Nordström, E., Lord, A., Tucker, S.M.E., et al. (2013). Monoclonal antibodies selective for α-synuclein oligomers/protofibrils recognize brain pathology in Lewy body disorders and α-synuclein transgenic mice with the disease-causing A30P mutation. Journal of Neurochemistry. 126 (1). 131-144.
Status: Published
Fagerqvist, T., Näsström, T., Ihse, E., Lindström, V., Sahlin, C., et al. (2013). Off-pathway α-synuclein oligomers seem to alter α-synuclein turnover in a cell model but lack seeding capability in vivo. Amyloid : Journal of Protein Folding Disorders. 20 (4). 233-244.
Status: Published

Report (Other academic)

Hylander, S., Axén, C., Fridolfsson, E., Green, M., Näsström, T. (2020). Tiaminbrist i Östersjöområdet. Havsmiljöinstitutet. 64.