Protein glycation is involved in structure and stability changes that impair protein functionality, which is associated with several human diseases, such as diabetes and amyloidotic neuropathies (Alzheimer's disease, Parkinson's disease and Andrade's syndrome). To understand the relationship of protein glycation with protein dysfunction, unfolding and beta-fibre formation, numerous studies have...

Non-enzymatic protein glycosylation (glycation) contributes to many diseases and aging of organisms. It can be expected that inhibition of glycation may prolong the lifespan. The search for inhibitors of glycation, mainly using in vitro models, has identified natural compounds able to prevent glycation, especially polyphenols and other natural antioxidants. Extrapolation of results of in vitro ...

advanced glycation end-products (ages) are formed by non-enzymatic reaction between reducing sugar and protein. ages play important roles in pathogenesis of diabetic, aging complications, endothelial dysfunction and neurological diseases such as the alzheimer’s disease. therefore compounds that prevent the glycation reaction are purported to have therapeutic effect on patients with diabetes and...

Diabetic patients in poor glycemic control show increased glycation of total plasma proteins, but little is yet known about the relative extents to which the various individual proteins are glycated. Thus, we studied the non-enzymic glycation of several major plasma proteins and plasma protein fractions in normal and diabetic patients. In vivo glycation for most plasma proteins was very low in ...

Protein glycation is an age-dependent posttranslational modification associated with several neurodegenerative disorders, including Alzheimer's and Parkinson's diseases. By modifying amino-groups, glycation interferes with folding of proteins, increasing their aggregation potential. Here, we studied the effect of pharmacological and genetic manipulation of glycation on huntingtin (HTT), the cau...

We have developed a colorimetric assay for determining the degree of glycation of serum proteins that is unaffected by glycosylation residues. This was accomplished by reducing the proteins with sodium borohydride prior to periodate oxidation. Previous periodate-based methods, which offer several advantages over other glycation assays, cannot determine glycoprotein glycation because interferenc...

Background: Glucose-induced protein glycation has been implicated in the progression of diabetic complications and age-related diseases. The anti-glycation potential of polyphenol-rich plant extracts has been shown previously. Bunium Persicum has been demonstrated to possess a high level of polyphenols. The aim of current in vitro study was to determine the possible inhibitory effect of Bunium ...