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Lipid-derived aldehydes accelerate light chain amyloid and amorphous aggregation.

Jorge Nieva¹, Asher Shafton, Laurence J Altobell

¹Department of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.

|June 27, 2008

Summary

Lipid-derived aldehydes accelerate antibody light chain (LC) aggregation, forming amyloid or amorphous deposits. This process, influenced by aldehyde type, can be inhibited by trimethylamine N-oxide (TMAO).

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Published on: April 26, 2018

Area of Science:

Biochemistry and Molecular Biology
Protein Misfolding Diseases
Immunology

Background:

Antibody light chain (LC) aggregation causes fatal AL-amyloidosis and light-chain deposition disease (LCDD).
Understanding molecular factors driving LC aggregation is crucial for disease pathology.
Physiologically relevant conditions and biologically derived molecules are key areas of investigation.

Purpose of the Study:

To investigate the in vitro aggregation of human kappa and lambda light chains.
To determine the effect of biologically relevant lipid-derived aldehydes on LC aggregation.
To characterize the structural and kinetic properties of aldehyde-induced LC aggregates.

Main Methods:

Incubation of human kappa (kappa-MJM) and lambda (lambda-L155) light chains with aldehydes (4-HNE, MDA, GLY, KA, ALD) under physiological conditions (PBS, pH 7.4, 37°C).
Thioflavin-T (ThT) and Congo Red (CR) binding assays to detect beta-sheet conformation.
Turbidity studies, Transmission Electron Microscopy (TEM) for aggregate morphology, and kinetic profiling.

Main Results:

Lipid-derived aldehydes accelerate LC aggregation, inducing secondary structure changes towards beta-sheet conformation.
Cholesterol secosterols (KA, ALD) induced amorphous, ThT/CR-negative aggregates, while 4-HNE, MDA, and GLY formed amyloidogenic, ThT/CR-positive aggregates.
Aldehyde type dictated aggregate morphology (amyloid vs. amorphous) and aggregation kinetics (nucleated polymerization vs. seeded aggregation).

Conclusions:

Aldehydes, particularly lipid-derived ones, significantly promote antibody light chain aggregation.
The specific aldehyde determines the type of aggregate formed (amyloid vs. amorphous) and the aggregation pathway.
This study extends the paradigm of inflammatory aldehyde-induced protein misfolding to antibody light chain aggregation.