Temperature-dependent β-sheet formation in β-amyloid Aβ1–40 peptide in water: uncoupling β-structure folding from aggregation
作者： Olga Gursky , Sergei Aleshkov
DOI: 10.1016/S0167-4838(99)00228-9
关键词: Hydrophobic effect 、 Monomer 、 Crystallography 、 Folding (chemistry) 、 Circular dichroism 、 Dimer 、 Protein folding 、 Beta sheet 、 Peptide 、 Chemistry
摘要: To probe the role of temperature in conversion soluble Alzheimer's beta-amyloid peptide (Abeta) to insoluble beta-sheet rich aggregates, we analyzed solution conformation Abeta(1-40) from 0 98 degrees C by far-UV circular dichroism (CD) and native gel electrophoresis. The CD spectra 15-300 microg/ml aqueous (pH approximately 4.6) at are concentration-independent suggest a substantially unfolded and/or unusually folded characteristic Abeta monomer or dimer. Heating 37 induces rapid reversible coil beta-strand transition that is independent concentration thus not linked oligomerization. Consequently, this may occur within Incubation leads slow concentration-dependent accumulation; heating 85 further folding Our results demonstrate importance thermal history for Abeta.
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