Computational Structural Analysis and Interaction Network Profiling of Lipases: Implications for Biomedical and Therapeutic Applications

Lipases are widely used enzymes that facilitate the process of breaking down triglycerides to glycerol and fatty acids and are involved in different processes of lipid metabolism, drug metabolism, the diagnosis of diseases, and several industrial processes. In this paper, a detailed computational work has been conducted to examine the structural determinants of the stability of organic solvents in lipases. An eighty-two-lipase dataset was obtained in the Protein Data Bank and assessed by amino acid composition profiling, stabilizing structural interactions, and calculation of physicochemical properties. The parameters such as the hydrophobic interactions, salt bridges, hydrogen bonds, and packing density were determined to determine factors that contributed to the stability of the solvents. The analysis of protein-protein interaction with the STRING database also revealed the functional association of the lipases in the different species (including Homo sapiens, Pan troglodytes, and Mus musculus). This study has limitations, however, in terms of its being based on computational analysis and the small number of experimentally characterized solvent-stable lipases that can be compared. Thus, experimental validation by mutagenesis, soluble stability experiments with enzymes, and rational protein engineering strategies should be undertaken in future efforts to improve solvent tolerance level depending on the structural characteristics observed. The results can inform the structural aspects of lipase stability and can be used in the future in the fields of biomedical studies, drug development, and enzyme engineering.