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• W4385200898 abstract "Amyloid formation is linked with serious human diseases that are currently incurable. Usually, in the study of amyloid aggregation, the description of the protein’s association is in focus. Whereas the mechanism of the cross-β-structure formation, and the presence of aggregation reversibility, remain insufficiently explored. In this work, the kinetics of amyloid aggregation of apomyoglobin (ApoMb) have been studied using thioflavin fluorescence, electron microscopy, and non-denaturing electrophoresis. An analysis of the concentration dependence of the aggregation rates allows the conclusion that ApoMb amyloid formation includes the stages of conformational rearrangements in the aggregates, followed by their association and the fibril formation. The study of the mutant variants aggregation kinetics showed that the association rate is determined by the amino acids’ hydrophobicity, while the rate of conformational rearrangements is affected by the localization of the substitution. An unexpected result was the discovery that ApoMb amyloid formation is reversible, and under native-like conditions, the amyloid can dissociate, producing monomers. A consequence of the reversibility of amyloid aggregation is the presence of the monomer after aggregation completion. Since the aggregation reversibility indicates the possibility of dissociation of already formed fibrils, presented data and approaches can be useful in finding ways for amyloid diseases treatment." @default.
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• W4385200898 date "2023-07-24" @default.
• W4385200898 modified "2023-09-27" @default.
• W4385200898 title "Association, Conformational Rearrangements and the Reverse Process of Aggregates Dissociation during Apomyoglobin Amyloid Formation" @default.
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• W4385200898 doi "https://doi.org/10.3390/physchem3030021" @default.
• W4385200898 hasPublicationYear "2023" @default.
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