Abstract
Cinnamic acid and its derivatives have shown a variety of pharmacologic properties. However, little is known about the antiglycation properties of cinnamic acid and its derivatives. The present study sought to characterize the protein glycation inhibitory activity of cinnamic acid and its derivatives in a bovine serum albumin (BSA)/fructose system. The results demonstrated that cinnamic acid and its derivatives significantly inhibited the formation of advanced glycation end products (AGEs) by approximately 11.96–63.36% at a concentration of 1 mM. The strongest inhibitory activity against the formation of AGEs was shown by cinnamic acid. Furthermore, cinnamic acid and its derivatives reduced the level of fructosamine, the formation of Nɛ-(carboxymethyl) lysine (CML), and the level of amyloid cross β-structure. Cinnamic acid and its derivatives also prevented oxidative protein damages, including effects on protein carbonyl formation and thiol oxidation of BSA. Our findings may lead to the possibility of using cinnamic acid and its derivatives for preventing AGE-mediated diabetic complications.
Highlights
Chronic hyperglycemia causes non-enzymatic protein glycation by reducing sugars, such as glucose and fructose, which react with the free amino groups of protein to initiate a complex cascade of repeated condensations, rearrangements, oxidative modifications, forming advanced glycation end products (AGEs) [1,2]
When the glycation occurred in the presence of cinnamic acid, we observed that cinnamic acid significantly reduced the formation of AGEs by 63.36 ± 1.07%, as compared to bovine serum albumin (BSA) incubated with fructose
The addition of fructose to the BSA solution for 28 days significantly increased the extent of protein carbonyl formation, compared to BSA in the absence of fructose. It found that cinnamic acid and its derivatives suppressed protein carbonyl formation by approximately 18.2–25.7% when compared to BSA incubated with fructose
Summary
Chronic hyperglycemia causes non-enzymatic protein glycation by reducing sugars, such as glucose and fructose, which react with the free amino groups of protein to initiate a complex cascade of repeated condensations, rearrangements, oxidative modifications, forming advanced glycation end products (AGEs) [1,2]. A comprehensive review of the current scientific literature reveals that the inhibition of AGE formation is one of the therapeutic approaches to prevent the progression of diabetic complications [6]. The trial was terminated because it has shown some toxicity problems in diabetic nephropathy, such as flu-like symptoms, gastrointestinal problems and anemia [7,8]. In this regard, the effort has been directed in finding effective phytochemical compounds from dietary plants, fruits and herbal medicines against protein glycation [9,10,11,12]
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