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Updated: Jun 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Structural alterations within native amyloidogenic immunoglobulin light chains.

Edward G Randles¹, James R Thompson, Douglas J Martin

¹Department of Biochemistry and Molecular Biology, College of Medicine, Mayo Clinic, Rochester, MN 55905, USA.

Journal of Molecular Biology

|April 14, 2009

Summary

This summary is machine-generated.

Structural insights into light chain amyloidosis (AL) reveal how protein misfolding and instability contribute to amyloid fibril formation in vital organs. This study highlights key alterations in AL proteins linked to disease.

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

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Last Updated: Jun 24, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Area of Science:

Biochemistry
Structural Biology
Medical Science

Background:

Amyloid diseases involve protein misfolding and fibril formation.
Light chain amyloidosis (AL) is characterized by immunoglobulin light chain amyloid deposition in organs.
AL proteins exhibit thermodynamic instability linked to increased fibril formation.

Purpose of the Study:

To elucidate the structural basis of amyloid formation in light chain amyloidosis.
To investigate the relationship between protein structure, somatic mutations, and instability in AL proteins.

Main Methods:

X-ray crystallography was used to determine the structures of two AL proteins (AL-12 and AL-103).
Structural analysis focused on the germ line dimer interface and flanking loops.
Results were correlated with the presence of somatic mutations in the studied proteins.

Main Results:

The crystal structures of AL-12 and AL-103 revealed retention of the canonical germ line dimer interface.
Significant structural alterations were identified in two loops adjacent to the dimer interface.
These alterations were linked to somatic mutations and likely contribute to protein instability.

Conclusions:

Identified structural alterations in AL proteins are associated with protein instability.
These structural changes may drive conformational alterations critical for initiating amyloid formation in AL.
Understanding these structural features offers insights into the pathogenesis of light chain amyloidosis.