Intramesoporous Silica Structure Differentiating Protein Loading Density
Journal Article
·
· Materials Letters, 75:102-106
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.
- Research Organization:
- Pacific Northwest National Laboratory (PNNL), Richland, WA (US)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1037526
- Report Number(s):
- PNNL-SA-81847; KC0201050; 400412000
- Journal Information:
- Materials Letters, 75:102-106, Journal Name: Materials Letters, 75:102-106 Vol. 75
- Country of Publication:
- United States
- Language:
- English
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