Incubation of Amyloidogenic Peptides in Reverse Micelles Allow Active Control of Oligomer Size and Study of Protein–Protein Interactions
Journal
ChemMedChem
Journal Volume
19
Journal Issue
23
ISSN
1860-7179
1860-7187
Date Issued
2024-09-17
Author(s)
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.
Subjects
Beta amyloid
Fibril nuclei
Liposomes
Solid-state NMR
Publisher
Wiley
Type
journal article