Structural Characterization of Proteins Adsorbed at Nanoporous Materials

Abstract

A nanoporous material has been applied for the development of functional nanobiomaterials by utilizing its uniform pore structure and large adsorption capacity. The structure and stability of biomacromolecules, such as peptide, oligonucleotide, and protein, are primary factors to govern the performance of nanobiomaterials, so that their direct characterization methodologies are in progress. In this review, we focus on recent topics in the structural characterization of protein molecules adsorbed at a nanoporous material with uniform meso-sized pores. The thermal stabilities of the adsorbed proteins are also summarized to discuss whether the structure of the adsorbed protein molecules can be stabilized or not.

Large-pore mesoporous silica: template design, thin film preparation and biomolecule infiltration

“…This results are in agreement with recent publication on myoglobin infiltration and condensation at pores entrance. 13,60 Results of infiltration of glutaminase and amino acid oxidase show an increased overlayer deposition close to the enzyme diameter. In case of urase the infiltration into the structure seems to be hindered and an overlayer thickness similar in value to the enzyme diameter was measured.…”

Designing Sites in Heterogeneous Catalysis: Are We Reaching Selectivities Competitive With Those of Homogeneous Catalysts?

“…Finally, porous solids are often used as supports in order to achieve high surface areas, sometimes even to retain big molecular discrete catalysts, enzymes in particular, within the solid to minimize leaching, but those pores may impose geometrical constrains on the ability of molecular catalysts to adopt their required structure and interact with the reactants for optimum promotion of reactions, especially with large molecular catalysts such as enzymes (as mentioned before, Section ). , To the specific limitations imposed by the local structure of the pores, additional consideration needs to be given to mass transport limitations of reactants and products to and from the catalytic site, although this is a problem common to all heterogeneous catalysts. It should be mentioned that the complexity of solid surfaces can also provide unique opportunities, since they can display large atomic assemblies difficult to reproduce via molecular synthesis.…”

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

“…Cylindrical nanopores have been applied in the development of artificial biocatalytic systems, − controlled drug release systems, artificial chaperones, and solid-state nanopore sensing devices . Because the conformation of a biomacromolecule, such as protein or DNA, is sensitive to its microenvironment and surface interactions at the pore wall, its correlation with the nanopore diameter is a key issue in such nanopore-based technologies. − The folding/unfolding properties of a monomeric biomacromolecule are an important part of conformational studies, and optimal nanopore diameters have been reported for enhancing the stability of the folded structures and the molecular chaperoning function of biomacromolecules …”