African Journal of
Pharmacy and Pharmacology

  • Abbreviation: Afr. J. Pharm. Pharmacol.
  • Language: English
  • ISSN: 1996-0816
  • DOI: 10.5897/AJPP
  • Start Year: 2007
  • Published Articles: 2279

Full Length Research Paper

To evaluate likely antiamyloidogenic property of ferulic acid and baicalein against human islet amyloid polypeptide aggregation, in vitro Study

Seyyed Mehdi Mirhashemi* and Mohammasd-Hossein Aarabi
Biochemistry Department, Faculty of Medicine, Kashan University of Medical Sciences, Kashan, I.R. Iran.
Email: [email protected]

  •  Accepted: 08 February 2012
  •  Published: 08 March 2012


Aggregation of human islet amyloid polypeptide (hIAPP) as islet amyloid is associated with increased beta cell apoptosis and reduced beta cell mass in type 2 diabetes mellitus. Inhibition of the formation of β-amyloid fibrils, as well as the destabilization of preformed β-amyloid in the pancreas, would be attractive therapeutic targets for the treatment of diabetes mellitus. Using fluorescence spectroscopic analysis with Thioflavin T, we examined the effects of Ferulic acid and Baicalein on the formation, and destabilization of β-amyloid in vitro. The results showed that after 192 h incubation by shaker incubator in 37°C, Ferulic acid at 10 and 40 µM repressed amylin amyloid formation by 22.6 and 27.7% respectively (p<0.05) and the similar values of Baicalein inhibited the formation of β-sheet structure by 20.4 and 30.9% respectively (p<0.05). The obtained data also confirmed that amyloidal sheet opening was induced by Ferulic acid and Baicalein significantly (p<0.05). It may conclude that islet amyloid cytotoxicity to β-cells may be reduced by these two herbal extracts and these compounds should be key molecules for the development of the therapeutics for Diabetes mellitus.


Key words: Amylin, diabetes, ferulic acid, baicalein, amylin fibrils.