Binding Affinity of Glucose to Glucose Dehydrogenase (GDH) at Binding Sites and Factors Affecting on Binding Affinity Using Molecular Docking

Abstract

Bioelectrochemical systems such as biosensors and biofuel cells employ enzymes as biocatalysts instead of conventional metal catalysts. In the recent past, these bioelectrochemical devices are being used in various application fields; for these devices, the design of protein with unique ligand binding functions carries significant capability for application in biomedicine and biotechnology. However, the capacity to create/filter ligand-binding proteins remains restricted and is mostly dependent on experimentation. The computation process might cut development costs while also allowing for thorough testing of our insight of the principles controlling molecular recognition. However, ligand affinity changes can be quantitatively predicted using computational methods when numerous parameters (temperature, pH, mutation) are altered. In this study, we have used molecular docking to estimate the glucose binding affinity to heterodimeric Flavin adenine dinucleotide-dependent glucose dehydrogenase gamma-alpha complex (GDHγα), a promising enzyme used in glucose monitoring systems. Then, we looked into how the effect of changing in factors affected binding affinity, which is directly related to enzyme activity. We investigated the extent to which these parameters influence binding affinity to the enzyme and, as a result, enzyme function. According to the findings, our enzyme has a higher binding affinity than the current glucose-detecting enzyme glucose oxidase GOX. This research contributes to a better understanding of the ligand-binding protein mechanism as well as the design and development of bioelectrochemical systems that use these biocatalysts.