PMID- 36729014 OWN - NLM STAT- MEDLINE DCOM- 20230606 LR - 20230614 IS - 1097-0134 (Electronic) IS - 0887-3585 (Linking) VI - 91 IP - 7 DP - 2023 Jul TI - Investigation of biological activities of two cultivars of Cicer arietinum proteins mass associated with Alzheimer's disease. PG - 859-871 LID - 10.1002/prot.26472 [doi] AB - 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 beta-amyloid peptide (betaA) 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) mug/mL, respectively, with no activity on BChE. The 50 mug/mL protein concentration of each cultivar suppressed betaA 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. CI - (c) 2023 Wiley Periodicals LLC. FAU - Mafakher, Ladan AU - Mafakher L AD - Thalassemia & Hemoglobinopathy Research center, Health research institute, Ahvaz Jundishapur University of Medical Sciences, Ahvaz, Iran. FAU - Rismani, Elham AU - Rismani E AD - Molecular Medicine Department, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. FAU - Saeedi, Mina AU - Saeedi M AD - Persian Medicine and Pharmacy Research Center, Tehran University of Medical Sciences, Tehran, Iran. FAU - Emami, Mir Mohammad Reza Hosseini Moghadam AU - Emami MMRHM AD - Department of Pharmacognosy, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. FAU - Hadjiakhoondi, Abbas AU - Hadjiakhoondi A AD - Department of Pharmacognosy, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. AD - Medicinal Plants Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. FAU - Najafi, Zahra AU - Najafi Z AD - Department of Medicinal Chemistry, School of Pharmacy, Hamedan University of Medical Sciences, Hamedan, Iran. FAU - Manayi, Azadeh AU - Manayi A AUID- ORCID: 0000-0002-0420-5930 AD - Medicinal Plants Research Center, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran. LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20230221 PL - United States TA - Proteins JT - Proteins JID - 8700181 RN - EC 3.1.1.7 (Acetylcholinesterase) RN - 0 (Amyloid beta-Peptides) RN - 0 (Cholinesterase Inhibitors) SB - IM MH - Humans MH - Aged MH - *Alzheimer Disease/drug therapy/metabolism MH - *Cicer/chemistry/metabolism MH - Acetylcholinesterase/metabolism MH - Molecular Docking Simulation MH - Amyloid beta-Peptides MH - Cholinesterase Inhibitors/pharmacology OTO - NOTNLM OT - SDS-PAGE OT - acetylcholinesterase OT - butyrylcholine esterase OT - chickpea OT - molecular docking OT - beta-Amyloid peptide EDAT- 2023/02/03 06:00 MHDA- 2023/06/06 06:42 CRDT- 2023/02/02 10:46 PHST- 2023/01/11 00:00 [revised] PHST- 2022/08/16 00:00 [received] PHST- 2023/01/30 00:00 [accepted] PHST- 2023/06/06 06:42 [medline] PHST- 2023/02/03 06:00 [pubmed] PHST- 2023/02/02 10:46 [entrez] AID - 10.1002/prot.26472 [doi] PST - ppublish SO - Proteins. 2023 Jul;91(7):859-871. doi: 10.1002/prot.26472. Epub 2023 Feb 21.