Phytochemical profile, enzyme inhibition activity and molecular docking analysis of<i>Feijoa sellowiana</i>O. Berg

Abstract

<i>Feijoa sellowiana</i> leaves and fruits have been investigated as a source of diverse bioactive metabolites. Extract and eight metabolites isolated from <i>F. sellowiana</i> leaves were evaluated for their enzymatic inhibitory activity against α-glucosidase, amylase, tyrosinase, acetylcholinestrerase and butyrylcholinesterase both <i>in vitro</i> and <i>in silico</i>. <i>Feijoa</i> leaves' extract showed strong antioxidant activity and variable levels of inhibitions against target enzymes with a strong anti-tyrosinase activity (115.85 mg Kojic acid equivalent/g). Additionally, α-tocopherol emerged as a potent inhibitor of AChE and BChE (5.40 & 10.38 mmol galantamine equivalent/g, respectively). Which was further investigated through molecular docking and found to develop key enzymatic interactions in AChE and BChE active sites. Also, primetin showed good anti BChE (11.70 mmol galantamine equivalent/g) and anti-tyrosinase inhibition (90.06 mmol Kojic acid equivalent/g) which was also investigated by molecular docking studies. Highlights Isolation of eight bioactive constituents from <i>Feijoa sellowiana</i> leaves. <i>In vitro</i> assays using different enzymatic drug targets were investigated. <i>In silico</i> study was performed to define compound interactions with target proteins. <i>Feijoa</i> leaf is an excellent source of anti-AChE and antityrosinase bioactives.