Abstract
The inhibitory activity of isoferulic acid (IFA) on fructose- and glucose-mediated protein glycation and oxidation of bovine serum albumin (BSA) was investigated. Our data showed that IFA (1.25–5 mM) inhibited the formation of fluorescent advanced glycation end products (AGEs) and non-fluorescent AGE [Nε-(carboxymethyl) lysine: CML], as well as the level of fructosamine. IFA also prevented protein oxidation of BSA indicated by decreasing protein carbonyl formation and protein thiol modification. Furthermore, IFA suppressed the formation of β-cross amyloid structures of BSA. Therefore, IFA might be a new promising anti-glycation agent for the prevention of diabetic complications via inhibition of AGEs formation and oxidation-dependent protein damage.
Highlights
Protein glycation is a non-enzymatic reaction between the carbonyl group of a reducing sugar and the free amino group of a protein
Protein glycation is a spontaneous chemical modification of proteins or amino acids by reducing monosaccharides such as glucose and fructose [15,25]. This reaction generates irreversible heterogeneous byproducts termed advanced glycation end products (AGEs) which are implicated in the development of aging as well as the pathogenesis of age-related disorders including Alzheimer’s disease and diabetes complications [26,27]
This is the first study to report the inhibitory effect of isoferulic acid (IFA) on fructose- and glucose-mediated bovine serum albumin (BSA) glycation
Summary
Protein glycation is a non-enzymatic reaction between the carbonyl group of a reducing sugar and the free amino group of a protein. The reaction initiates a complex cascade of repeated condensations, rearrangements, and oxidative modifications, resulting in the reversible formation of a characteristic structure called a Schiff’s base [1,2] This is further rearranged into more stable structures called Amadori products, which undergo further oxidation, generating dicarbonyl compounds to form cross-linked structures termed advanced glycation end products or AGEs [3,4]. AGEs play a vital role in further cross-linking or modification of other proteins and generating oxidizing intermediates, resulting in induction of oxidative stress in vascular cells as well as other tissues [7] For this reason, the excessive formation of AGEs and their accumulation in the tissues is a significant contributor to age-related diseases [8] and diabetic complications such as retinopathy, nephropathy and neuropathy [9]. The study examined the effects of IFA on oxidation-dependent damage to BSA and formation of CML in vitro
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