title: Intramesoporous silica structure differentiating protein loading density.
abstract: We report that hydrothermal aging temperature had a critical effect on intramesoporous structure of mesoporous silica and thus the intramesoporous structure affected protein loading in the mesoporous silica significantly. For a neutral protein Immunoglobulin G with a Y-like molecular shape, the larger desorption pore size allowed the larger protein loading. For a charged protein glucose oxidase with an elliptical molecular shape, the larger surface area resulted in the larger protein loading. Fluorescence emission spectra from tyrosinyl and tryptophanyl residues of the proteins in mesoporous silicas indicated that the charged protein was electrostatically attached inside the mesopores in a way of monolayer, while the neutral protein IgG could continue to aggregate after the monolayer occupancy.
authors: Pacific Northwest National Laboratory, P. O. Box 999, Richland, WA 99352, USA.
authors: Wen
authors: W
authors: Qi
authors: Xiaolin
authors: X
authors: Li
authors: Baowei
authors: B
authors: Chen
authors: Pei
authors: P
authors: Yao
authors: Chenghong
authors: C
authors: Lei
authors: Jun
authors: J
authors: Liu