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Daniel Otzen


Daniel Otzen

Professor Interdisciplinary Nanoscience Center - INANO-MBG, iNANO-huset

Keywords

  • Protein-Fatty Acid Complexes
  • Membrane Protein Folding
  • Protein-(bio)surfactant complexes
  • Molecular basis of functional and pathological protein self-assembly and aggregation
  • Stability and dynamics of membrane proteins
  • Biophysics of protein-surfactant interactions
  • Cryophilic enzymes
  • Novel uses for plant proteins and small metabolites
  • Self-assembly of functional amyloid

Head of Protein Biophysics Group

Professor Daniel Otzen
PhD in Protein Biophysics

Protein aggregation: the dark side of the force

We strive to understand in molecular detail how protein aggregates are formed in sickness and in health. This knowledge is used to combat neurodegenerative diseases and other misfolding disorders as well as to develop self-assembling material. We also study protein interactions with lipids and membranes.

We study how proteins associate to form fibrils amyloid fibrils and oligomers. We focus on a-synuclein (involved in Parkinson’s disease), proteins in corneal dystrophy, storage of peptide hormones as aggregates, and functional bacterial amyloid. We investigate by spectroscopy, light-scattering and calorimetry how aggregation can be controlled and inhibited by small molecules and surface-active compounds.

We have extensive collaborations with experts in small-angle X-ray scattering, mass spectrometry and cellular fibrillation. As a consequence, we build up a detailed view of the steps involved in aggregation and their physiological consequences and of the highly controlled formation of functional amyloid. We also study protein self-assembly promoted by free fatty acids, forming protein-lipid complexes called liprotides, which can store and transport hydrophobic drugs and nutraceuticals. Another topic in our group is the folding of proteins inside the membrane environment. We complement our experimental data with computational studies.

We collaborate with industry and academia to develop new ways of targeting the cytotoxic and generally deleterious consequences of protein aggregation and exploit the potential of liprotides.

Recent publications