Protein Condensation at Nanopore Entrances as Studied by Differential Scanning Calorimetry and Small-Angle Neutron Scattering.

The condensation of globular myoglobin (Mb) at the pore entrances of mesoporous silica (MPS) with a series of pore diameters (4.2, 6.4, 7.7, and 9.0 nm) was examined by differential scanning calorimetry (DSC) and contrast-matching small-angle neutron scattering (CM-SANS) experiments. The DSC measurements were performed to estimate the amount of Mb adsorbed at two different adsorption sites, namely, the pore interior and the pore entrance regions. The CM-SANS measurements were conducted to observe condensation of Mb molecules at the pore entrance regions. Notably, the nanopore entrance with a diameter close to twice that of the Mb diameter was found to be the specific cavity to facilitate the condensation of globular Mb. The Mb condensation occurred at the entrances of the 6.4 nm pore during the adsorption uptake from concentrated Mb solutions, whereas the adsorption uptake from diluted Mb solutions induced the condensation of Mb at the entrances of the 7.7 nm pore.