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In JoVE (1)
- Near Infrared Optical Projection Tomography for Assessments of β-cell Mass Distribution in Diabetes Research
Other Publications (2)
Articles by Nils Norlin in JoVE
Near Infrared Optical Projection Tomography for Assessments of β-cell Mass Distribution in Diabetes Research
Anna U. Eriksson*1, Christoffer Svensson*1, Andreas Hörnblad1, Abbas Cheddad1, Elena Kostromina1, Maria Eriksson1, Nils Norlin1, Antonello Pileggi2, James Sharpe3, Fredrik Georgsson4, Tomas Alanentalo1, Ulf Ahlgren1
1Umeå Centre for Molecular Medicine, Umeå University, 2Cell Transplant Center, Diabetes Research Institute, University of Miami,, 3EMBL-CRG Systems Biology Program, Centre for Genomic Regulation, Catalan Institute of Research and Advanced Studies, 4Dept. of Computing Science, Umeå University
Other articles by Nils Norlin on PubMed
Physical Chemistry Chemical Physics : PCCP. Apr, 2007 | Pubmed ID: 17431522
An extended FÃ¶rster theory (EFT) on electronic energy transfer is presented for the quantitative analysis of time-resolved fluorescence lifetime and depolarisation experiments. The EFT, which was derived from the stochastic Liouville equation, yields microscopic information concerning the reorientation correlation times, the order parameters, as well as inter chromophoric distances. Weakly interacting donor and acceptor groups, which reorient and interact in a pair wise fashion, are considered, under isotropic and anisotropic conditions. For the analysis of experiments it is shown that not only do we need to consider the orientational distributions of the transition dipoles, but the internal reorienting molecular dynamics within the pair which is of even greater importance. The latter determines the shape as well as the rate of the observed donor fluorescence and depolarisation decays, which are most often not mono-exponential functions. It is shown that the commonly used FÃ¶rster theory is a special case of the EFT. Strategies are presented for applying the EFT, which makes use of Brownian dynamics simulation.
Aggregation and Fibril Morphology of the Arctic Mutation of Alzheimer's AÎ² Peptide by CD, TEM, STEM and in Situ AFM
Journal of Structural Biology. Oct, 2012 | Pubmed ID: 22750418
Morphology of aggregation intermediates, polymorphism of amyloid fibrils and aggregation kinetics of the "Arctic" mutant of the Alzheimer's amyloid Î²-peptide, AÎ²((1-40))(E22G), in a physiologically relevant Tris buffer (pH 7.4) were thoroughly explored in comparison with the human wild type Alzheimer's amyloid peptide, wt-AÎ²((1-40)), using both in situ atomic force and electron microscopy, circular dichroism and thioflavin T fluorescence assays. For arc-AÎ²((1-40)) at the end of the 'lag'-period of fibrillization an abrupt appearance of â‰ˆ 3 nm size 'spherical aggregates' with a homogeneous morphology, was identified. Then, the aggregation proceeds with a rapid growth of amyloid fibrils with a variety of morphologies, while the spherical aggregates eventually disappeared during in situ measurements. Arc-AÎ²((1-40)) was also shown to form fibrils at much lower concentrations than wt-AÎ²((1-40)): â‰¤ 2.5 Î¼M and 12.5 Î¼M, respectively. Moreover, at the same concentration, 50 Î¼M, the aggregation process proceeds more rapidly for arc-AÎ²((1-40)): the first amyloid fibrils were observed after c.a. 72 h from the onset of incubation as compared to approximately 7 days for wt-AÎ²((1-40)). Amyloid fibrils of arc-AÎ²((1-40)) exhibit a large variety of polymorphs, at least five, both coiled and non-coiled distinct fibril structures were recognized by AFM, while at least four types of arc-AÎ²((1-40)) fibrils were identified by TEM and STEM and their mass-per-length statistics were collected suggesting supramolecular structures with two, four and six Î²-sheet laminae. Our results suggest a pathway of fibrillogenesis for full-length Alzheimer's peptides with small and structurally ordered transient spherical aggregates as on-pathway immediate precursors of amyloid fibrils.