Oncocalyxone A functions as an anti-glycation agent in vitro

PLoS One. 2015 Jun 25;10(6):e0131222. doi: 10.1371/journal.pone.0131222. eCollection 2015.

Abstract

Advanced glycation endproducts (AGE) are the result of post-translational changes to proteins, which ultimately compromise their structure and/or function. The identification of methods to prevent the formation of these compounds holds great promise in the development of alternative therapies for diseases such as diabetes. Plants used in traditional medicine are often rich sources of anti-glycation agents. Therefore, in this study, we investigated the anti-glycation activity of one such compound, Oncocalyxone A (Onco A). Using spectrofluorimetric techniques, we determined that Onco A inhibits AGE formation in a concentration-dependent manner. Its IC50 value (87.88 ± 3.08 μM) was almost two times lower than the standard anti-glycation compound aminoguanidine (184.68 ± 4.85 μM). The excellent anti-glycation activity of Onco A makes it an exciting candidate for the treatment of diseases associated with excessive accumulation of AGE. However, additional studies are necessary to identify its mechanism of action, as well as the in vivo response in suitable model organisms.

MeSH terms

  • Animals
  • Anthraquinones / chemistry*
  • Anthraquinones / pharmacology
  • Brazil
  • Cattle
  • Dose-Response Relationship, Drug
  • Drug Evaluation, Preclinical
  • Fructose / chemistry
  • Glucose / chemistry
  • Glycation End Products, Advanced / chemistry*
  • Glycosylation
  • Inhibitory Concentration 50
  • Medicine, Traditional
  • Plant Extracts / chemistry
  • Serum Albumin, Bovine / chemistry
  • Spectrometry, Fluorescence

Substances

  • Anthraquinones
  • Glycation End Products, Advanced
  • Plant Extracts
  • oncocalyxone A
  • Serum Albumin, Bovine
  • Fructose
  • Glucose

Grants and funding

The authors have no support or funding to report.