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Stability of Proteins on Hydrophilic Surfaces
- Source :
- Langmuir. 31:1005-1010
- Publication Year :
- 2015
- Publisher :
- American Chemical Society (ACS), 2015.
-
Abstract
- The physical and chemical properties of solid substrates or surfaces critically influence the stability and activity of immobilized proteins such as enzymes. Reports of increased stability and activity of enzymes near/on surfaces as compared with those in solution abound; however, a mechanistic understanding is wanting. Simulations and experiments are used here to provide details toward such a mechanistic understanding. Experiments demonstrate increased activity of alcohol dehydrogenase (ADH) inside moderate hydrophilic mesopourous silica (SBA-15) pores but drastically decreased activity inside very hydrophilic NH2-SBA-15 surfaces as compared with that in solution. Also, the temperature stability of ADH was increased over that in solution when immobilized in a cavity with a mildly hydrophilic surface. Simulations confirm these experimental findings. Simulations calculated in the framework of a hydrophobic-polar (H-P) lattice model show increased thermal stability of a model 64-mer peptide on positive and zero curvature surfaces over that in solution. Peptides immobilized inside negative curvature cavities (concave) with hydrophilic surfaces exhibit increased stability only inside pores that are only 3-4 nm larger than the hydrodynamic radius of the peptide. Peptides are destabilized, however, when the surface hydrophilic character inside very small cavities/pores becomes large.
- Subjects :
- Saccharomyces cerevisiae Proteins
Hydrodynamic radius
Surface Properties
Kinetics
Peptide
Saccharomyces cerevisiae
Curvature
Adsorption
Enzyme Stability
Electrochemistry
General Materials Science
Thermal stability
Immobilized proteins
Spectroscopy
Enzyme Assays
chemistry.chemical_classification
Chromatography
Alcohol Dehydrogenase
Temperature
Surfaces and Interfaces
Enzymes, Immobilized
Silicon Dioxide
Condensed Matter Physics
Solutions
chemistry
Chemical engineering
Thermodynamics
Negative curvature
Peptides
Hydrophobic and Hydrophilic Interactions
Subjects
Details
- ISSN :
- 15205827 and 07437463
- Volume :
- 31
- Database :
- OpenAIRE
- Journal :
- Langmuir
- Accession number :
- edsair.doi.dedup.....1f820b54e640da42e2626af689824b65