Heat-induced amyloid-like aggregation of β-lactoglobulin affected by glycation by α-dicarbonyl compounds in a model study.

BACKGROUND

α-Dicarbonyl compounds are widely generated in the Maillard reaction, caramelization and oil oxidation during heat treatment. These compounds can readily react with lysine and arginine residues of a protein, whereas the influence of these compounds on protein structure and quality has seldom been revealed. This study compared influence of glycation by glucose and α-dicarbonyl compounds on amyloid-like aggregation of β-lactoglobulin (β-LG), both fibrillation kinetics and conformation of aggregates were studied.

RESULTS

Compared with glycation by glucose, the glycation by α-dicarbonyl compounds resulted in faster reduction of free amino group, sulfydryl group, and the relative content of β-sheet secondary structure, according to the ultraviolet (UV) spectra or circular dichroism (CD) spectra results. Based on the analysis of fibrillation kinetics using thioflavin T (ThT) binding assay, the glycation by α-dicarbonyls were more efficient in suppressing the growth of fibrillar aggregates. In addition, glycation by α-dicarbonyl resulted in amorphous oligomers, which were compared with the amyloid-like aggregates in control and glucose-glycated samples, based on the transmission electron microscopy (TEM) observation.

CONCLUSIONS

Glycation by α-dicarbonyl compounds induced larger decline in the β-sheet structure of β-LG than glycation by glucose, and thus largely suppressed the amyloid-like aggregation of β-LG and changed the morphology of aggregates. © 2019 Society of Chemical Industry.