Protein adsorption induced bridging flocculation: the dominant entropic pathway for nano-bio complexation

• Published in: Nanoscale Vol. 8; no. 6; pp. 3326 - 3336
• Main Authors: Eren, Necla Mine, Narsimhan, Ganesan, Campanella, Osvaldo H
• Format: Journal Article
• Language: English
• Published: England 14.02.2016
• Subjects: Adsorption; Animals; Binding; Chickens; Complexation; Dichroism; Entropy; Flocculation; Gain; Muramidase - chemistry; Nanoparticles - chemistry; Nanostructure; Silicon Dioxide - chemistry; Surface chemistry
• ISSN: 2040-3364; 2040-3372
• DOI: 10.1039/c5nr06179b

Lysozyme-silica interactions and the resulting complexation were investigated through adsorption isotherms, dynamic and electrophoretic light scattering, circular dichroism (CD), and isothermal titration calorimetry (ITC). A thermodynamic analysis of ITC data revealed the existence of two binding modes during protein-nanoparticle complexation. Both binding modes are driven by the cooperation of a favorable enthalpy in the presence of a dominating entropy gain. The first binding mode has a higher binding affinity, a lower equilibrium stoichiometry and is driven by a higher entropic contribution compared to the second type. The observed favorable enthalpy gain in both modes is attributed to non-covalent complexation whereas the entropy gain is associated with the re-organization of the silica surface including not only the solvent and counter ion release, but also the protein's conformational changes. Possible mechanisms are proposed to explain non-covalent complexations for each binding mode by relating the changes in the zeta potential and hydrodynamic radius to the obtained adsorption isotherms and calorimetry profile. Based on all these findings, it is proposed that lysozyme adsorption on nano-silica is the result of protein-nanoparticle and protein-protein interactions that further leads to spontaneous, non-directional and random complexation of silica through bridging flocculation.