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ABSTRACT: Background
The specificity of protein functions depends on its folding ability into a functional structure. Protein folding is an essential systemic phenomenon that prevents incorrect folding which could result in harmful aggregation. This harmful aggregation of proteins causes neurodegenerative diseases and systemic amyloidosis. Experimental and theoretical approaches were used in this study to explicate the probable mechanisms of action of quercetin in inhibition of glucose-induced glycation through estimations of percentage glycated protein, inhibited induced protein aggregation, and unoxidized bovine serum albumin thiol groups and assessments of molecular interactions of quercetin with the structures of bovine serum albumin, amyloid beta-peptide (1-42) and 3D amyloid-beta (1-42
SUBMITTER: Oso BJ
PROVIDER: S-EPMC10654330 | biostudies-literature | 2023 Nov
REPOSITORIES: biostudies-literature