Semi-quantification and Potency Verification of the HIV Protease Inhibitor Based on the Matrix-Capsid Protein Immobilized Nickel (II)/NTA-Tol/Graphene Oxide/SPCE Electrochemical Biosensor

by Selleckchem | Sep 15 2023

Human immunodeficiency virus (HIV) causing acquired immune deficiency syndrome (AIDS) is still a global issue. Long-term drug treatment and nonadherence to medication increase the spread of drug-resistant HIV strains. Therefore, the identification of new lead compounds is being investigated and is highly desirable. Nevertheless, a process generally necessitates a significant budget and human resources. In this study, a simple biosensor platform for semi-quantification and verification of the potency of HIV protease inhibitors (PIs) based on electrochemically detecting the cleavage activity of the HIV-1 subtype C-PR (C-SA HIV-1 PR) was proposed. An electrochemical biosensor was fabricated by immobilizing His6-matrix-capsid (H6MA-CA) on the electrode surface via the chelation to Ni2+-nitrilotriacetic acid (NTA) functionalized GO. The functional groups and the characteristics of modified screen-printed carbon electrodes (SPCE) were characterized by Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and energy-dispersive X-ray spectroscopy (EDS). C-SA HIV-1 PR activity and the effect of PIs were validated by recording changes in electrical current signals of the ferri/ferrocyanide redox probe. The detection of PIs, i.e., lopinavir (LPV) and indinavir (IDV), toward the HIV protease was confirmed by the decrease in the current signals in a dose-dependent manner. In addition, our developed biosensor demonstrates the ability to distinguish the potency of two PIs to inhibit C-SA HIV-1 PR activities. We anticipated that this low-cost electrochemical biosensor would increase the efficiency of the lead compound screening process and accelerate the discovery and development of new HIV drugs.

Comments:

The passage describes a study proposing a simple biosensor platform for the semi-quantification and verification of the potency of HIV protease inhibitors (PIs). The goal of the study is to address the global issue of HIV/AIDS by identifying new lead compounds for drug treatment.

The biosensor platform utilizes an electrochemical method to detect the cleavage activity of the HIV-1 subtype C protease (C-SA HIV-1 PR). The biosensor is constructed by immobilizing a protein called His6-matrix-capsid (H6MA-CA) on the electrode surface through chelation to Ni2+-nitrilotriacetic acid (NTA) functionalized graphene oxide (GO). The modified screen-printed carbon electrodes (SPCE) used in the biosensor are characterized using Fourier transform infrared (FTIR) spectroscopy, scanning electron microscopy (SEM), and energy-dispersive X-ray spectroscopy (EDS).

To validate the activity of C-SA HIV-1 PR and the effect of PIs, changes in electrical current signals of the ferri/ferrocyanide redox probe are recorded. The presence of PIs, such as lopinavir (LPV) and indinavir (IDV), leads to a decrease in current signals in a dose-dependent manner, indicating the inhibition of the HIV protease.

Furthermore, the developed biosensor has the capability to distinguish the potency of different PIs in inhibiting C-SA HIV-1 PR activities. The authors expect that this low-cost electrochemical biosensor will enhance the efficiency of the lead compound screening process, facilitating the discovery and development of new HIV drugs.

In summary, the study presents a novel biosensor platform that utilizes electrochemical detection to assess the potency of HIV protease inhibitors. This approach offers a cost-effective solution for screening potential lead compounds and expediting the search for new HIV treatments.