Alzheimers 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 Alzheimers in the future,
although more experimental work is needed in this issue.