Molecular Biology Reports

, Volume 38, Issue 3, pp 1617–1620

Trans-chalcone: a novel small molecule inhibitor of mammalian alpha-amylase

  • Mahmoud Najafian
  • Azadeh Ebrahim-Habibi
  • Nastaran Hezareh
  • Parichehreh Yaghmaei
  • Kazem Parivar
  • Bagher Larijani
Article

DOI: 10.1007/s11033-010-0271-3

Cite this article as:
Najafian, M., Ebrahim-Habibi, A., Hezareh, N. et al. Mol Biol Rep (2011) 38: 1617. doi:10.1007/s11033-010-0271-3
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Abstract

Trans-chalcone (1,3-diphenyl-2-propen-1-one), a biphenolic core structure of flavonoids precursor was tested for inhibitory activity toward alpha-amylase. Porcine pancreatic alpha-amylase was observed to be effectively inhibited by this compound, which showed competitive behavior with a Ki of 48 μM. Soluble starch (the natural substrate of the enzyme) was used in this study in order to obtain more realistic results. The possible binding mode of the compound was assessed in silico, and the two residues Trp59, and Tyr62 were proposed as main interacting residues with trans-chalcone. In conclusion, this compound could be used to design effective inhibitors of alpha-amylase.

Keywords

Trans-chalcone1,3-Diphenyl-2-propen-1-oneAlpha-amylaseInhibitorDiabetes

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Mahmoud Najafian
    • 1
  • Azadeh Ebrahim-Habibi
    • 2
  • Nastaran Hezareh
    • 2
  • Parichehreh Yaghmaei
    • 1
  • Kazem Parivar
    • 1
  • Bagher Larijani
    • 2
  1. 1.Science and Research Branch Islamic Azad UniversityTehranIran
  2. 2.Endocrinology and Metabolism Research CenterTehran University of Medical SciencesTehranIran