A Novel Enzyme Based Spr-Biosensor to Detect Bromocriptine As an Ergoline Derivative Drug Publisher



Jabbari S¹ ; Dabirmanesh B¹ ; Arab SS² ; Amanlou M³ ; Daneshjou S¹ ; Gholami S¹ ; Khajeh K¹ Show Affiliations
Source: Sensors and Actuators# B: Chemical Published:2017

Abstract

In the modern biomedical and therapeutic drug monitoring technology, development of high performance sensing methods for ergoline derivative drug, bromocriptine (BC), is a critical issue due to its plasma low concentration and important function in Parkinson's disease. The results of the protein-ligand docking simulation consistent with competitive inhibition experimental study strongly support the binding of BC to the laccase active site. Therefore, a new biosensor for direct label-free detection of BC is presented based on surface plasmon resonance (SPR) using laccase from Bacillus sp. HR03 as a recognition element. The biosensor chip surface was constructed by covalent immobilization of the laccase on a SPR carboxymethyl dextran surface. The calculated kinetic affinity (KD) was 5.4 nM, which indicated the high affinity between BC and the immobilized laccase. The biosensor could determine BC in a linear detection range from 0.001 ng/ml to 1000 ng/ml with a lower detection limit of 0.001 ng/ml. The biosensor provided acceptable specificity with suitable recovery in simulated blood samples. This new biosensor represents a novel, fast, sensitive, economic cost effective and accurate method for the therapeutic monitoring and detection of the BC. © 2016 Elsevier B.V.