In Silico Mutagenesis, Docking, and Molecular Dynamics: Their Role in Biosensor Design for Environmental Analysis and Monitoring

Biosensor design is an active area of research that spans several disciplines and techniques ranging from biotechnology to nanotechnology. In the former, it is often the case that de novo design is shunned in favor of redesigning an existing protein. In the present chapter, we will focus on the latter strategy and emphasize its application on a protein from cow milk, β-lactoglobulin (BLG). BLG is a protein component of ungulates’ milk. It is present in cow, goat, and sheep; their milk is widely consumed by humans. Human milk lacks this protein entirely. It is a small protein made up by β-sheets and containing, at least, two disulfide bridges. It can form homodimers; it can monomerize or oligomerize depending on conditions such as pH, protein concentration, and others. Its binding site is unique due to its hydrophobicity. As far as structural information shows, this binding site is a cavity that is exposed to the solvent but not occupied by it. Considering this information, it should be no surprise that BLG binds fatty acids and liposoluble vitamins. While BLG’s biological function is unknown, its hydrophobic binding site can potentially bind other hydrophobic compounds such as medicines, pesticides, or even persistent organic pollutants. Thus, understanding of the physicochemical properties of BLG, its binding site, and its engineering and redesign could lead to biosensors to monitor hydrophobic pollutants.