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Updated: Jun 18, 2025

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Incubation of Amyloidogenic Peptides in Reverse Micelles Allow Active Control of Oligomer Size and Study of
Han-Wen Chang1, Chien-I Yang1, Jerry Chun Chung Chan1
1Department of Chemistry, National Taiwan University, No.1, Section 4, Roosevelt Road, Taipei, 10617, Taiwan.
Abstract:
Studies of the structure and dynamics of oligomeric aggregates of amyloidogenic peptides pose challenges due to their transient nature. This concept article provides a brief overview of various nucleation mechanisms with reference to the classical nucleation theory and illustrates the advantages of incubating amyloidogenic peptides in reverse micelles (RMs). The use of RMs not only facilitates size regulation of oligomeric aggregates but also provides an avenue to explore protein-protein interactions among the oligomeric aggregates of various amyloidogenic peptides. Additionally, we envision the feasibility of preparing brain tissue-derived oligomeric aggregates using RMs, potentially advancing the development of monoclonal antibodies with enhanced potency against these pathological species in vivo.
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