Abstract
The aim of this work was to determine the structural requirements for peptides that inhibit acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) activities. The data set used consisted of 19 oligopeptides that had been identified through mass spectrometry analysis of enzymatic digests of yellow field pea protein. The structure-function relationship was analyzed by partial least squares regression using the 5z scores. A nine-component model was created from 16 peptides for AChE inhibitory peptides (Q2 = 67.2% and R2 = 0.9974), while three data sets were prepared for BuChE inhibitory peptides to improve the quality of the models (Q2 = 26.7-46.4% and R2 = 0.9577-0.9958). The most active peptides from the PLS models have threonine, leucine, alanine, and valine at the N terminal, asparagine, histidine, proline, and arginine at the second position, with aspartic acid and serine at the third, and arginine at the C terminal.
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