Confinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering

• DOI: 10.1021/jacs.8b08454
• Publication Date: 2018-09-27T16:44:59Z
• Authors: Justin Siefker; Ralf Biehl; Margarita Kruteva; Artem Feoktystov; Marc-Olivier Coppens
• Keywords: Models, Molecular; Drug Carriers; info:eu-repo/classification/ddc/540; Myoglobin; Protein Stability; Proteins; Silicon Dioxide; 01 natural sciences; 0104 chemical sciences; Neutron Diffraction; Protein Aggregates; Drug Delivery Systems; Scattering, Small Angle; Humans; Muramidase; Porosity

While mesoporous silicas have been shown to be a compelling candidate for drug delivery and the implementation of biotechnological applications requiring protein confinement immobilization, understanding behavior upon physical adsorption into silica pores is limited. Many indirect methods are available assess general adsorbed stability, such as Fourier-transform infrared spectroscopy activity assays. However, limitation these that spatial arrangement within cannot assessed. Mesoporous pose distinct challenge direct methods, transmission electron microscopy, which lacks contrast resolution required adequately observe immobilized structure, nuclear magnetic resonance, computationally intensive requires knowledge primary structure priori. Small-angle neutron scattering can surmount limitations pores. Hereby, we stabilization fluid-like arrangement, facilitated by geometry-dependent crowding effects in cylindrical ordered silica, SBA-15. Stabilization induced from factor, observed samples at maximum loading SBA-15 with pore diameters 6.4 8.1 nm. Application this effect prevention irreversible aggregation high concentration environments proposed.