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  • Title: Heat-induced amyloid-like aggregation of β-lactoglobulin affected by glycation by α-dicarbonyl compounds in a model study.
    Author: Zhao D, Zhang X, Xu D, Su G, Li B, Li C.
    Journal: J Sci Food Agric; 2020 Jan 30; 100(2):607-613. PubMed ID: 31591730.
    Abstract:
    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.
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