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Related Experiment Video

Updated: Oct 13, 2025

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Dynamic protein structures in normal function and pathologic misfolding in systemic amyloidosis.

Emily Lewkowicz¹, Olga Gursky¹

¹Boston University School of Medicine, Department of Physiology & Biophysics, W302, 700 Albany St, Boston, MA 02118, USA.

Biophysical Chemistry

|November 13, 2021

Summary

This summary is machine-generated.

Dynamic protein regions are vital for function but can cause amyloid disease. This review explores how these regions balance beneficial roles with pathologic amyloid formation in human plasma proteins.

Keywords:

Apolipoproteins Flexible and disordered protein regions Immunoglobulin light chain Proteolysis and misfolding Serum amyloid A Systemic amyloidosis

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Area of Science:

Biochemistry
Structural Biology
Molecular Medicine

Background:

Dynamic and disordered protein regions are crucial for biological functions like ligand binding and signaling.
These same regions can lead to protein misfolding and amyloid fibril deposition, contributing to diseases.

Purpose of the Study:

To review the dual role of dynamic and disordered regions in protein function and amyloid formation.
To examine how these regions contribute to systemic amyloidoses using specific human plasma protein families.

Main Methods:

Review of existing literature on protein structure, stability, and dynamics.
Analysis of immunoglobulin light chain, apolipoproteins, and serum amyloid A families.
Examination of amyloidogenic variants and their altered dynamics.

Main Results:

Dynamic regions offer functional advantages but also present liabilities for amyloidogenesis.
Mechanisms include destabilizing native structure, promoting aggregation, or facilitating cleavage into aggregation-prone fragments.
Enhanced protein dynamics can also accelerate degradation, counteracting amyloid accumulation.

Conclusions:

The balance between functional dynamics and amyloidogenic potential is critical.
Amyloidogenic mutations or post-translational modifications can shift this balance.
Understanding these dynamics is key to comprehending systemic amyloidoses and developing therapeutic strategies.