Butyrylcholinesterase inhibitory activity of peptides identified from yellow field pea (Pisum sativum) enzymatic protein hydrolysates

Abstract

Butyrylcholinesterase (BuChE) is an enzyme implicated in Alzheimer’s disease due to the excessive breakdown of neurotransmitters. The study screened and synthesized de novo peptides derived from yellow field pea as BuChE activity inhibitors. The conformational changes of the enzyme were evaluated to confirm interaction with the peptides, along with mode of inhibition by the peptide and their binding affinity. The result showed no significant conformational changes of the enzyme after interaction with peptides. The catalytic parameters were low indicating strong affinity at low peptide concentrations and maximum velocity (Vmax) decreased with increasing peptide concentration for all the peptides. Peptides with mixed inhibition mode had low docking energy scores suggesting high affinity for BuChE and peptide-enzyme interaction were through catalytic triad and /or peripheral anionic site. Results revealed that peptides derived from yellow field pea protein could be potential inhibitors of BuChE activity and probably effective in AD therapy.

Keywords

• Butyrylcholinesterase
• Peptide
• Inhibition
• Kinetics
• Molecular docking
• Alzheimer’s disease