In vitro acetylcholinesterase activity of peptide derivatives isolated from two species of Leguminosae

Abstract

Context: Cratylia mollis Martius ex Benth. and Cenostigma macrophyllum Tul. (Leguminosae) are both endemic Brazilian plants and they are used by the natives as medicinal plants, and the leaves of C. mollis are also employed as forage for cattle during the dry season of region.

Objective: Isolation of the compounds responsible for the acetylcholinesterase (AChE) inhibition from the CHCl₃ active extract.

Materials and methods: Two peptidic compounds were isolated by chromatographic techniques from the CHCl₃ extract of the leaves of C. mollis and C. macrophyllum. They were identified by spectrometric data analysis (MS and NMR) and they were subjected to AChE inhibition employing Ellman’s test.

Results: The peptides were identified as N-benzoylphenylalaninoyl-phenlyalaninolacetate (aurentiamide acetate) (1) and N-benzoylphenylalaninyl-N-benzoylphenylalaninate (2). Both peptides 1 and 2 exhibit AChE inhibition, with IC₅₀ values equal to 111.34 µM and 137.6 µM, respectively.

Discussion and conclusion: Compound 1 (aurentiamide acetate) has rarely been isolated from the Leguminosae family, and N-benzoylphenylalaninyl-N-benzoylphenylalaninate (2) is a compound that has never previously been isolated from this family. Compound 1 is shown to be a potent inhibitor of AChE, with IC₅₀ values similar to the physostigmine control (141.51 µM).

• Aurentiamide acetate
• Cenostigma macrophyllum
• Cratylia mollis
• Leguminosae
• N-benzoylphenylalaninyl-N-benzoylphenylalaninate