Search results for "Trifluoroethanol"
showing 4 items of 4 documents
Trifluoroethanol modulates α-synuclein amyloid-like aggregate formation, stability and dissolution
2016
The conversion of proteins into amyloid fibrils and other amyloid-like aggregates is closely connected to the onset of a series of age-related pathologies. Upon changes in environmental conditions, amyloid-like aggregates may also undergo disassembly into oligomeric aggregates, the latter being recognized as key effectors in toxicity. This indicates new possible routes for in vivo accumulation of toxic species. In the light of the recognized implication of α-Synuclein (αSN) in Parkinson's disease, we present an experimental study on supramolecular assembly of αSN with a focus on stability and disassembly paths of such supramolecular aggregate species. Using spectroscopic techniques, two-pho…
Existence of metastable intermediate lysozyme conformation highlights the role of alcohols in altering protein stability.
2011
Alcohols have a manifold effect on the conformational and thermodynamic stability of native proteins. Here, we study the effect of moderate concentrations of trifluoroethanol (TFE) on the thermal stability of hen egg-white lysozyme (HEWL), by far-UV circular dichroism and by steady-state and time-resolved photoluminescence of intrinsic tryptophans. Our results highlight that TFE affects lysozyme stability by preferential solvation of the protein molecule. Furthermore, we discovered the existence at 20% TFE of an equilibrium partially folded state of lysozyme, intermediate between the native and the unfolded state. A three-state model is therefore used to interpolate the thermal denaturation…
CCDC 966310: Experimental Crystal Structure Determination
2014
Related Article: Moritz Schubert, Jana Leppin, Kathrin Wehming, Dieter Schollmeyer, Katja Heinze and Siegfried R. Waldvogel|2014|Angew.Chem.,Int.Ed.|53|2494|doi:10.1002/anie.201309287
Modulation of α-Synuclein Aggregation Process and Fibril Stability by Co-solvents
2014
Amyloid fibrils are involved in several amyloid-related pathologies such as Parkinson's disease, Alzheimer's disease and type II diabetes. As a result, scientific community is nowadays addressing considerable efforts towards the comprehension of fibrillation mechanisms, particularly focusing on how they are affected by environmental conditions, small molecules and/or membrane presence. In this scenario, alpha-synuclein (aSN), a small protein involved in Parkinson's disease, represents a challenging model system for studying aggregation phenomena, and understanding the pathogenesis at molecular level. Indeed, it is poorly understood how fibril formation is linked to the progressive neurodege…