Stability of Proteins Confined in MCM-48 Mesoporous Molecular Sieves – The Effects of pH, Temperature and Co-solvents
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Shuang Zhao
Our approach was to encapsulate the model protein ribonuclease A (RNase A) in mesoporous silica MCM-48 (Mobil Composition of Matter No. 48) with glasslike wall structure and well-defined pores to create a confined hydrophilic microenvironment. The differential scanning calorimetric (DSC) method was employed to evaluate the stability of the confined protein as a function of pH and at various co-solvent conditions. Due to a significant stabilization effect, the immobilized protein exhibits a large shift (about 28 ºC at pH 5.5) in the unfolding temperature in confined space of about 25 Å. The stabilization against temperature-induced unfolding is further enhanced with the protein immobilized at higher pH, and the maximum loading of protein has been observed near its isoelectric point. It was also found that the addition of kosmotropic (glycerol) and chaotropic (urea) co-solvents has different impacts on protein immobilization and unfolding scenario.
© Oldenbourg Wissenschaftsverlag
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- Controlled Release of Proteins Bound to Spherical Polyelectrolyte Brushes
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- Stability of Proteins Confined in MCM-48 Mesoporous Molecular Sieves – The Effects of pH, Temperature and Co-solvents
- Hydrogen Bonding of Water Confined in Controlled-Pore Glass 10-75 Studied by 1H-Solid State NMR
Articles in the same Issue
- Bunsen Colloquium: Controlling Protein Adsorption at Materials Surfaces
- Adsorption of Collagen Fragments on Titanium Oxide Surfaces: A Molecular Dynamics Study
- Adsorption of the Flexible Salivary Proteins Statherin and PRP-1 to Negatively Charged Surfaces – A Monte Carlo Simulation and Ellipsometric Study
- Surface-Tethered Polymers to Influence Protein Adsorption and Microbial Adhesion
- Lactoperoxidase and Histatin 5 – their Adsorption Behaviour on Silica and Hydrophobized Silica Surfaces, and Implications on their Role in the Initial Salivary Film Formation
- Ultrasensitive Fluorescence Microscopy Studies of Protein Interactions with Functionalized Surfaces
- Adsorption of Amyloid β (1-40) Peptide at Liquid Interfaces
- Controlled Release of Proteins Bound to Spherical Polyelectrolyte Brushes
- In-Situ-ATR-FTIR Detection of Protein Sorption at Polyelectrolyte Multilayers: Variation of the Thickness
- Stability of Proteins Confined in MCM-48 Mesoporous Molecular Sieves – The Effects of pH, Temperature and Co-solvents
- Hydrogen Bonding of Water Confined in Controlled-Pore Glass 10-75 Studied by 1H-Solid State NMR
