Isoferulic acid, a new anti-glycation agent, inhibits fructose- and glucose-mediated protein glycation in vitro

• Author(s) / Creator(s)

  • Meeprom, Aramsri
  • Adisakwattana, Sirichai
  • Sompong, Weerachat
  • Chan, Catherine B.

• 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.

• Date created

  2013

• Subjects / Keywords

  • Nε-(Carboxymethyl)Lysine
  • Fructosamine
  • Isoferulic Acid
  • Protein Oxidation
  • Advanced Glycation End Products
  • Protein Glycation

• Type of Item

  Article (Published)

• DOI

  https://doi.org/10.7939/R3HM52Z7C

• License

  Attribution-NonCommerical-ShareALike 4.0 International