title: Isoferulic acid, a new anti-glycation agent, inhibits fructose- and glucose-mediated protein glycation in vitro.
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.
authors.affiliation: Program in Clinical Biochemistry and Molecular Medicine, Department of Clinical Chemistry, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand. Jamaea_p@hotmail.com
authors.forename: Aramsri
authors.initials: A
authors.lastname: Meeprom
authors.forename: Weerachat
authors.initials: W
authors.lastname: Sompong
authors.forename: Catherine B
authors.initials: CB
authors.lastname: Chan
authors.forename: Sirichai
authors.initials: S
authors.lastname: Adisakwattana
mesh_terms: D002934:Cinnamates / Q000737:chemistry / Q000494:pharmacology*; D005632:Fructose / Q000737:chemistry*; D005947:Glucose / Q000737:chemistry*; D017127:Glycation End Products, Advanced / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation / Q000187:drug effects; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000737:chemistry / Q000378:metabolism
chemical_list: D002934:Cinnamates; D017127:Glycation End Products, Advanced; D011506:Proteins; D012710:Serum Albumin, Bovine; D005632:Fructose; D005947:Glucose; C008180:isoferulic acid