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Diverse Structural Conversion and Aggregation Pathways of Alzheimerʼs Amyloid-β (1-40)
Lin, Yuxi,Sahoo, Bikash R.,Ozawa, Daisaku,Kinoshita, Misaki,Kang, Juhye,Lim, Mi Hee,Okumura, Masaki,Huh, Yang Hoon,Moon, Eunyoung,Jang, Jae Hyuck,Lee, Hyun-Ju,Ryu, Ka-Young,Ham, Sihyun,Won, Hyung-Sik American Chemical Society 2019 ACS NANO Vol.13 No.8
<P>Complex amyloid aggregation of amyloid-β (1-40) (Aβ<SUB>1-40</SUB>) in terms of monomer structures has not been fully understood. Herein, we report the microscopic mechanism and pathways of Aβ<SUB>1-40</SUB> aggregation with macroscopic viewpoints through tuning its initial structure and solubility. Partial helical structures of Aβ<SUB>1-40</SUB> induced by low solvent polarity accelerated cytotoxic Aβ<SUB>1-40</SUB> amyloid fibrillation, while predominantly helical folds did not aggregate. Changes in the solvent polarity caused a rapid formation of β-structure-rich protofibrils or oligomers <I>via</I> aggregation-prone helical structures. Modulation of the pH and salt concentration transformed oligomers to protofibrils, which proceeded to amyloid formation. We reveal diverse molecular mechanisms underlying Aβ<SUB>1-40</SUB> aggregation with conceptual energy diagrams and propose that aggregation-prone partial helical structures are key to inducing amyloidogenesis. We demonstrate that context-dependent protein aggregation is comprehensively understood using the macroscopic phase diagram, which provides general insights into differentiation of amyloid formation and phase separation from unfolded and folded structures.</P> [FIG OMISSION]</BR>