We investigated protein glycation in a complex milk system under controlled conditions representative of real-life consumer products, analysing intermediate and final products from skim powder production, aged samples. combined protein-centric LC-MS(/MS) with peptide-centric multi-protease LC-MS/MS focusing on the six most abundant bovine proteins. This strategy resulted identification glycated...

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...

The reaction between reducing sugars and protein free amines, known as the Maillar reaction results in the formation of advanced glycation endproducts (AGEs). AGE modification changes the structure of proteins to amyloid cross-beta structure. These protein structures can activate receptors known as RAGE on glial cells (microglia and astrocytes), and induce the expression of inducible nitric oxi...

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...

Protein glycation adducts, early glycation adducts, such as N(epsilon)-fructosyl-lysine, and advanced glycation end products (AGEs) are uremic toxins. Glycation adducts are found in plasma and tissue proteins (glycation adduct residues), in peptides (glycation adduct peptide residues), and glycated amino acids (glycation free adducts). The latter two analyte groups arise from proteolysis of gly...

Abstract Glycation is a spontaneous post-translational modification of lysine, arginine, and the N-terminus proteins. Protein glycation closely related to pathogenesis human diseases, including diabetes, Alzheimer’s disease, renal cancer. The levels advanced end products (AGEs) are positively correlated with progression many diseases. However, it remains challenging analyze glycation-related pr...

Piper betle Linn. is a Pan-Asiatic plant having several beneficial properties. Protein glycation and advanced glycation end products (AGEs) formation are associated with different pathophysiological conditions, including diabetes mellitus. Our study aims to find the effect of methanolic extract of P. betle leaves on in vitro protein glycation in bovine serum albumin (BSA)-glucose model. The ext...

Several studies have indicated the presence of increased oxidative stress as a critical feature in the pathogenesis of chronic obstructive pulmonary disease (COPD). Another biochemical complication leading to pathogenesis is protein glycation. The nexus between oxidative stress and protein glycation in various pathological conditions is being unraveled. Increased oxidative stress can lead to en...

Glycation is a nonenzymatic process in which proteins react with reducing sugar molecules. The identification of glycation sites in protein may provide guidelines to understand the biological function of protein glycation. In this study, we developed a computational method to predict protein glycation sites by using the support vector machine classifier. The experimental results showed that the...

Vitamin C, an antioxidant substance soluble in water, can react with amino groups of proteins to form schiff bases. As diabetes leads to glycation of various protein which has effect on structure and biochemical activity of them, the inhibition of this process seems very vital. For several years researches in this field have done their best to recognize the antidiabetics compounds. The aim of t...