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Medicinal Chemistry Research

, Volume 27, Issue 6, pp 1559–1577 | Cite as

Inhibitor discovery from pomegranate rind for targeting human salivary α-amylase

  • Jiachen Sun
  • Shengjie Dong
  • Yueting Wu
  • Hui Zhao
  • Xia Li
  • Wenyuan Gao
Original Research
  • 115 Downloads

Abstract

This study explored the effects of the main active compounds of the pomegranate (Punica granatum L.) rind extract on the activity of the human salivary α-amylase and their molecular inhibitory mechanisms. Four compounds exhibited remarkable inhibitory activities against α-amylase, including (1) rutin, (2) luteolin, (3) quercetin, and (4) kaempferol. The IC50 values were found to be 265.65, 59.67, 99.56, and 139.72 μM for rutin, luteolin, quercetin, and kaempferol, respectively. The kinetic study using the Lineweaver–Burk revealed the four compounds showed a non-competitive inhibition against α-amylase. However, the exact localization of the binding site and the potentiation mechanism at the molecular level are presently unknown. We have performed the “blind docking” of four compounds on the human salivary α-amylase. The molecular modeling demonstrated a high affinity and tight binding capacity of these compounds at the binding site of α-amylase, where the Glu 233 was supposed to play a key role in exerting the inhibition activity of these compounds. The results may provide an important insight for the applications of computational methods in the drug design with treating disorders of carbohydrate metabolism.

Keywords

Pomegranate rind Human salivary α-amylase Inhibition activity Molecular docking Molecular dynamics simulation 

Notes

Acknowledgements

This work was supported by grants from the National Natural Science Foundation of China (NO. 81173487, 81373904 and 81673535), Science and Technology Program of China (NO. 2014FY111100) and Special Scientific Research of Chinese Medicine Industry (NO. 201307008).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

44_2018_2164_MOESM1_ESM.pdf (1.2 mb)
Supplementary Information

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Tianjin University of Traditional Chinese MedicineTianjinChina
  2. 2.School of Pharmaceutical Science and TechnologyTianjin UniversityTianjinChina
  3. 3.Faculty of General EducationGuangdong Baiyun UniversityGuangzhouChina
  4. 4.Department of PhysicsTianjin Normal UniversityTianjinChina

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