2. Academic Validation
  3. Inhibition behavior of Sennoside A and Sennoside C on amyloid fibrillation of human lysozyme and its possible mechanism

Inhibition behavior of Sennoside A and Sennoside C on amyloid fibrillation of human lysozyme and its possible mechanism

  • Int J Biol Macromol. 2021 May 1:178:424-433. doi: 10.1016/j.ijbiomac.2021.02.213.
Wen Gao 1,  Li Jin 2,  Chunhong Liu 2,  Ning Zhang 3,  Ruiyan Zhang 4,  Zuzana Bednarikova 5,  Zuzana Gazova 5,  Anirban Bhunia 6,  Hans-Christian Siebert 7,  Huijun Dong 8
Affiliations

Affiliations

  • 1 Department of Pharmacy, Liaocheng University, Liaocheng, Shandong 252000, China.
  • 2 Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng, Shandong 252000, China.
  • 3 Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng, Shandong 252000, China. Electronic address: zhangning1111@126.com.
  • 4 Institute of Biopharmaceutical Research, Liaocheng University, Liaocheng, Shandong 252000, China. Electronic address: zry147896@163.com.
  • 5 Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, Slovakia.
  • 6 Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), 700054 Kolkata, India.
  • 7 RI-B-NT Research Institute of Bioinformatics and Nanotechnology, Franziusallee 177, 24148 Kiel, Germany.
  • 8 Department of Pharmacy, Liaocheng University, Liaocheng, Shandong 252000, China. Electronic address: donghuijun_747@163.com.
PMID: 33662415 DOI: 10.1016/j.ijbiomac.2021.02.213
Abstract

Amyloid proteins were recognized as the crucial cause of many senile diseases. In this study, the inhibitory effects of Sennoside A (SA) and Sennoside C (SC) on amyloid fibrillation were evaluated by the combination of biophysical approaches and molecular docking tool using human lysozyme (HL) as amyloid-forming model. The results of thioflavin-T (ThT), 8-anilino-1-naphthalenesulfonic acid (ANS) and congo red (CR) assays indicated that both SA and SC could inhibit the amyloid fibrillation of HL in a dose-dependent manner. The IC50 value of SA and SC on HL fibrillation was 200.09 μM and 186.20 μM, respectively. These findings were further verified by transmission electron microscopy (TEM) and atomic force microscopy (AFM), which showed that the addition of SA or SC could sharply reduce the amyloid fibrillation of HL. Additionally, the interactions of HL with SA and SC were investigated by steady-state fluorescence spectra and molecular docking studies. The results suggested that both SA and SC could bind to the binding pocket of HL and form a stable complex mainly via hydrogen bonds, van-der-Waals forces and hydrophobic interactions. In conclusion, our experiments revealed that both SA and SC can significantly inhibit amyloid fibrillation of HL.

Keywords

Amyloid fibrillation; Sennoside A; Sennoside C.

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