Surface Plasmon Resonance Based Biosensor for Discovery of New Matrix Metalloproteinase-9 Inhibitors Publisher



Salehabadi H¹ ; Khajeh K² ; Dabirmanesh B² ; Biglar M³ ; Mohseni S⁴ ; Amanlou M^{1, 3}
Source: Sensors and Actuators# B: Chemical Published:2018

Abstract

In this study, inhibitory activity of 30 traditional medicinal plant extracts were examined and evaluated against MMP-9 activity by an orthogonal screening method based on an enzyme inhibition assay along with a surface plasmon resonance (SPR)-based binding assay. Five extracts exhibited reasonable inhibitory activity using inhibition assay. The most potent inhibition was found in Onopordum acanthium L. extract. Therefore, its active compound (onopordia) was isolated and identified as a new MMP-9 inhibitor. In order to evaluate binding profile of O. acanthium extract and onopordia, MMP-9 was immobilized on SPR carboxymethyldextran chip. Equilibrium constant (KD), maximum binding capacity (Rmax) and ΔGbinding values for the interaction of onopordia and MMP-9 were found to be 3 nM, 1190 μRIU and −51.37 kJ/mol. Docking analysis supported the strong binding of onopordia to the MMP-9 active site. This new SPR based biosensor could represent a simple, sensitive, real time and label-free method for screening medicinal plant extracts for identifying potential MMP-9 inhibitors in short time. © 2018 Elsevier B.V.