Association, Conformational Rearrangements and the Reverse Process of Aggregates Dissociation during Apomyoglobin Amyloid Formation

Amyloid formation is linked with serious human diseases that are currently incurable. Usually, in the study of amyloid aggregation, description protein’s association focus. Whereas mechanism cross-β-structure formation, and presence aggregation reversibility, remain insufficiently explored. In this work, kinetics apomyoglobin (ApoMb) have been studied using thioflavin fluorescence, electron microscopy, non-denaturing electrophoresis. An analysis concentration dependence rates allows conclusion ApoMb includes stages conformational rearrangements aggregates, followed by their fibril formation. The mutant variants showed rate determined amino acids’ hydrophobicity, while affected localization substitution. unexpected result was discovery reversible, under native-like conditions, can dissociate, producing monomers. A consequence reversibility monomer after completion. Since indicates possibility dissociation already formed fibrils, presented data approaches be useful finding ways for treatment.