Tuning Electrostatic Interactions To Control Orientation of GFP Protein Adsorption on Silica Surface

The adsorption of green fluorescent protein (GFP) onsilica surfaceshas been the subject of growing interest due to its potential applicationsin various fields, including biotechnology and biomedicine. In thisstudy, we used all-atom molecular dynamics simulations to investigatethe charge-driven adsorption of wild type GFP and its superchargedvariants on silica surfaces. The results showed that the positivelycharged variant of GFP adsorbed on the negatively charged silica surfacewith minimal loss in its secondary structure. Further studies wereconducted to understand the role of surface charge distribution ontwo other positively charged variants of GFP, and the results showedthat the orientation of GFP on silica can be easily tuned by carefulmutations of the charged amino acid residues on the GFP. This studyprovides valuable molecular insights into the role of electrostatic-drivenadsorption of GFP and highlights the importance of charge interactionsin the adsorption process.