title: Specific Interactions of Neutral Side Chains of an Adsorbed Protein with the Surface of α-Quartz and Silica Gel.
abstract: Many key features of the protein adsorption on the silica surfaces still remain unraveled. One of the open questions is the interaction of nonpolar side chains with siloxane cavities. Here, we use nonequilibrium molecular dynamics simulations for the detailed investigation of the binding of several hydrophobic and amphiphilic protein side chains with silica surface. These interactions were found to be a possible driving force for protein adsorption. The free energy gain was larger for the disordered surface of amorphous silica gel as compared to α-quartz, but the impact depended on the type of amino acid. The dependence was analyzed from the structural point of view. For every amino acid an enthalpy-entropy compensation behavior was observed. These results confirm a hypothesis of an essential role of hydrophobic interactions in protein unfolding and irreversible adsorption on the silica surface.
authors.affiliation: †Photochemistry Center, Russian Academy of Sciences, Novatorov street 7a, building 1, Moscow 119421, Russia.
authors.forename: Alexey V
authors.initials: AV
authors.lastname: Odinokov
authors.affiliation: †Photochemistry Center, Russian Academy of Sciences, Novatorov street 7a, building 1, Moscow 119421, Russia.|‡Moscow Engineering Physics Institute, Kashirskoe hwy 31, Moscow 115409, Russia.
authors.forename: Alexander A
authors.initials: AA
authors.lastname: Bagaturyants
mesh_terms: D000327:Adsorption; D056004:Molecular Dynamics Simulation; D011506:Proteins / Q000737:chemistry*; D011791:Quartz / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013499:Surface Properties; D013816:Thermodynamics
chemical_list: D011506:Proteins; D011791:Quartz; D012822:Silicon Dioxide