Ultrasensitive electrochemical determination of the cancer biomarker protein sPD-L1 based on a BMS-8-modified gold electrode

This work describes the modification of a gold electrode with the BMS-8 compound that interacts with the Programmed Death-Ligand 1 (PD-L1), an immune checkpoint protein. The results show that we can confirm the presence of the sPD-L1 in the concentration range of 10(-18) to 10(-8) M using electrochemical impedance spectroscopy (EIS) with a limit of detection (LOD) of 1.87 x 10(-14) M for PD-L1 (S/N = 3.3) and at a concentration of 10(-14) M via cyclic voltammetry (CV). Additionally, high-resolution X-ray photoelectron spectroscopy (XPS), contact angle, and surface free energy measurements were applied to confirm the functionalization of the electrode. We investigated the selectivity of the electrode for other proteins: Programmed Death-1 (PD-1), cluster of differentiation 160 (CD160), and B- and T-lymphocyte attenuator (BTLA) at concentrations of 10(-8) M. Differentiation between PD-L1 and PD-1 was achieved based on the analysis of the capacitance effect frequency dispersion at the surface of the modified Au electrode with BMS-8 after incubation at various concentrations of PD-L1 and PD-1 proteins in the range of 10(-18) to 10(-8) M. Significant differences were observed in the heterogeneity of PD-L1 and PD-1. The results of the quasi-capacitance studies demonstrate that BMS-8 strongly and specifically interacts with the PD-L1 protein. (C) 2021 Elsevier B.V. All rights reserved.

Automated summary

This study successfully demonstrates the modification of a gold electrode with BMS-8 compound for interaction with PD-L1, and further investigates the selectivity of the electrode for other proteins. The work provides a new approach for electrochemical detection of immune checkpoint proteins.