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Investigation of Biological Activities of Two Cultivars of Cicer Arietinum Proteins Mass Associated With Alzheimer's Disease Publisher Pubmed



Mafakher L1 ; Rismani E2 ; Saeedi M3 ; Emami MMRHM4 ; Hadjiakhoondi A4, 5 ; Najafi Z6 ; Manayi A5
Authors
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Authors Affiliations
  1. 1. Thalassemia & Hemoglobinopathy Research center, Health research institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran
  2. 2. Molecular Medicine Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran
  3. 3. Persian Medicine and Pharmacy Research Center, Tehran University of Medical Sciences, Tehran, Iran
  4. 4. Department of Pharmacognosy, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Medicinal Plants Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
  6. 6. Department of Medicinal Chemistry, School of Pharmacy, Hamedan University of Medical Sciences, Hamedan, Iran

Source: Proteins: Structure# Function and Bioinformatics Published:2023


Abstract

Alzheimer's disease (AD) is the most common cause of dementia in the elderly, with some known classical factors. Cicer arietinum (Leguminosae) is a source of protein for humans and contains albumin, globulin, glutelin, and prolamin. The protein content of two cultivars of C. arietinum, Hashem and Mansour, was isolated to evaluate their inhibition activity against acetylcholinesterase (AChE), butyrylcholine esterase (BChE), and β-amyloid peptide (βA) aggregation. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and molecular docking were also applied to evaluate the content and determine the potential of each chickpea protein to interact with AChE, respectively. Obtained data showed that proteins from both cultivars could inhibit AChE with IC50 of 17.73 (0.03) and 22.20 (0.06) μg/mL, respectively, with no activity on BChE. The 50 μg/mL protein concentration of each cultivar suppressed βA accumulation (Mansour: 25.66% and Hashem: 21.69%) and showed biometal chelating activity. SDS-PAGE analysis revealed relatively different protein patterns, though the Mansour cultivar contained some protein bands with molecular weights of 18, 24, and 70 kDa were estimated to belong to vicilin and legumin, which were absent in the Hashem protein mass. Molecular docking showed that legumin and especially vicilin have good potential to interact with AChE. The chickpea proteins showed inhibitory activity against AChE, which might be due to the vicilin and legumin fractions. The characterization of the inhibitory effect of each protein band could be promising in finding new therapeutic peptide candidates to treat Alzheimer's in the future, although more experimental work is needed in this issue. © 2023 Wiley Periodicals LLC.
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