A5081762364- Alzheimer's disease research and treatments
- Protein Structure and Dynamics
- Trace Elements in Health
- Drug Transport and Resistance Mechanisms
- Computational Drug Discovery Methods
- Supramolecular Self-Assembly in Materials
- Advanced NMR Techniques and Applications
- Prion Diseases and Protein Misfolding
- Molecular spectroscopy and chirality
- Lipid Membrane Structure and Behavior
- Aluminum toxicity and tolerance in plants and animals
- Biochemical effects in animals
- Cholinesterase and Neurodegenerative Diseases
- S100 Proteins and Annexins
- NMR spectroscopy and applications
- Advanced MRI Techniques and Applications
- Chemical Synthesis and Analysis
- Electron Spin Resonance Studies
- Neuroblastoma Research and Treatments
- Enzyme Structure and Function
- Radioactive element chemistry and processing
- Metabolomics and Mass Spectrometry Studies
- Enzyme function and inhibition
- Advanced biosensing and bioanalysis techniques
- Receptor Mechanisms and Signaling
Stockholm University
2016-2025
National Institute of Chemical Physics and Biophysics
2014-2023
Norwegian Womens Public Health Association
2021
Scripps Research Institute
2005
Estonian Academy of Sciences
1989-1990
Pro-inflammatory S100A9 protein is increasingly recognized as an important contributor to inflammation-related neurodegeneration. Here, we provide insights into specific mechanisms of action in Alzheimer's disease (AD). Due its inherent amyloidogenicity contributes amyloid plaque formation together with Aβ. In traumatic brain injury (TBI) itself rapidly forms plaques, which were reactive oligomer-specific antibodies, but not Aβ and fibrillar antibodies. They may serve precursor-plaques for...
Cigarette smoking is a significant risk factor for Alzheimer's disease (AD), which associated with extracellular brain deposits of amyloid plaques containing aggregated amyloid-β (Aβ) peptides. Aβ aggregation occurs via multiple pathways that can be influenced by various compounds. Here, we used AFM imaging and NMR, fluorescence, mass spectrometry to monitor in vitro how affected the cigarette-related compounds nicotine, polycyclic aromatic hydrocarbons (PAHs) one five rings, metal ions...
Protein misfolding and formation of cross-β structured amyloid fibrils are linked to many neurodegenerative disorders. Although recently developed quantitative approaches have started reveal the molecular nature self-assembly fibril proteins peptides, it is yet unclear how these self-organization events precisely modulated by microenvironmental factors, which known strongly affect macroscopic aggregation properties. Here, we characterize explicit effect ionic strength on microscopic rates β...
Abstract PFG‐NMR methods were used to measure the translational diffusion coefficients for Aβ peptide involved in Alzheimer's disease and also a series of fragments this peptide. The peptides ranged from pentamer full length Aβ(1–40). They studied at 25° C physiological pH aqueous solution. measured coefficients, including those known monomeric peptides, fitted without systematic deviations scaling law function molecular mass. We concluded that under these conditions Aβ(1–40) is form. From...
The temperature‐induced structural transitions of the full length Alzheimer amyloid β‐peptide [Aβ(1–40) peptide] and fragments it were studied using CD 1 H NMR spectroscopy. peptide undergoes an overall transition from a state with prominent population left‐handed 3 (polyproline II; PII)‐helix at 0 °C to random coil 60 °C, average ΔH 6.8 ± 1.4 kJ·mol −1 per residue, obtained by fitting Zimm–Bragg model data. is noncooperative for shortest N‐terminal fragment Aβ(1–9) weakly cooperative...
The amyloid beta peptide (Abeta) with 39-42 residues is the major component of plaques found in brains Alzheimer's disease patients, and soluble oligomeric aggregates mediate toxic effects on neurons. Abeta aggregation involves a conformational change structure to beta-sheet. In present study, we report effect detergents transitions Abeta, mimic that biomembranes may have. vitro, monomeric Abeta(1-40) dilute aqueous solution weakly structured. By gradually adding small amounts sodium dodecyl...
Amyloid proteins and peptides are a major contributing factor to the development of various neurodegenerative disorders, including Alzheimer’s prion diseases. Previously, designed cell-penetrating peptide (CPP) comprising hydrophobic signal sequence followed by protein (PrP)-derived polycationic (PrP23–28: KKRPKP) was shown have potent anti-prion properties. Here, we extend this approach toward amyloid-beta (Aβ) amyloid formation, which is associated with disease. We characterized...
The Alzheimer peptide fragment Aβ(12−28) was studied at millimolar concentration by parallel experiments with high-resolution nuclear magnetic resonance (NMR) and circular dichroism (CD) in solution a pH close to the isoelectric point of peptide. A preparation procedure using low temperature ionic strength buffer gave sample stable reproducible properties. Reversible changes secondary structure state aggregation were variation temperature. High-temperature promotes β-sheet induction, whereas...
Transportan is a 27-residue peptide (GWTLN SAGYL LGKIN LKALA ALAKK IL-amide) which has the ability to penetrate into living cells carrying hydrophilic load. chimeric constructed from 12 N-terminal residues of galanin in N-terminus with 14-residue sequence mastoparan C-terminus and connecting lysine. Circular dichroism studies transportan show that both peptides have close random coil secondary structure water. Sodium dodecyl sulfate (SDS) micelles induce 60% helix 75% mastoparan. The 600 MHz...
The dynamics of monomeric Alzheimer Aβ(1–40) in aqueous solution was studied using heteronuclear NMR experiments. 15N relaxation rates amide groups report on the peptide chain and make it possible to estimate structural propensities from temperature-dependent data chemical shifts change analysis. persistence length polypeptide determined a model which influence neighboring residue is assumed decay exponentially as function distance. monomer found decrease eight three residues when...
The amphiphilic nature of the amyloid-β (Aβ) peptide associated with Alzheimer's disease facilitates various interactions biomolecules such as lipids and proteins, effects on both structure toxicity peptide. Here, we investigate these peptide–amphiphile by experimental computational studies Aβ(1–40) in presence surfactants varying physicochemical properties. Our findings indicate that electrostatic peptide–surfactant are required for coclustering induction strength interaction depends...
In Alzheimer's disease, amyloid-β (Aβ) plaques and tau neurofibrillary tangles are the two pathological hallmarks. The co-occurrence combined reciprocal effects of Aβ protein aggregation have been observed in animal models disease. However, molecular mechanism their interaction remain unknown. Using a variety biophysical measurements, we here show that native full-length solubilizes Aβ40 peptide prevents its fibrillation. delays amyloid fibrillation at substoichiometric ratios, showing...
<title>Abstract</title> Mercury (Hg) exposure is a possible risk factor for Alzheimer´s disease (AD), and some studies have found higher Hg levels in AD patients. Yet, the evidence inconclusive, mechanism linking to neuropathology remains be found. The hallmark of brains deposits insoluble amyloid plaques consisting mainly aggregated amyloid-β (Aβ) peptides. Here, we use transmission electron microscopy (TEM) biophysical spectroscopy techniques study <italic>in vitro</italic> interactions...
Alzheimer's disease involves progressive neuronal loss. Linked to the is amyloid β (Aβ) peptide, a 38-43-amino acid peptide found in extracellular plaques brain. Cyclodextrins are nontoxic, cone-shaped oligosaccharides with hydrophilic exterior and hydrophobic cavity making them suitable hosts for aromatic guest molecules water. β-Cyclodextrin consists of seven α-d-glucopyranoside units has been shown reduce level fibrillation neurotoxicity Aβ. We have studied interaction between Aβ...