ArticleBiophysical journal2010
Thermal and structural stability of adsorbed proteins.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 41 citations in OpenAlex.
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- Diphtheria toxin T-domain as a tool for inducing lipid vesicle fusion.Communications chemistry · 2025Article
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- Poly(norepinephrine)-Mediated Universal Surface Modification for Patterning Human Pluripotent Stem Cell Culture and Differentiation.ACS biomaterials science & engineering · 2024Article
- Microbial Lipases and Their Potential in the Production of Pharmaceutical Building Blocks.International journal of molecular sciences · 2022Review
- Protein crystal nucleation in pores.Scientific reports · 2017Article
- Determining the role of missense mutations in the POU domain of HNF1A that reduce the DNA-binding affinity: A computational approach.PloS one · 2017Article
- Interplay of Coil-Globule Transition and Surface Adsorption of a Lattice HP Protein Model.The journal of physical chemistry. B · 2014Article
- Quantification of the influence of protein-protein interactions on adsorbed protein structure and bioactivity.Colloids and surfaces. B, Biointerfaces · 2013Article
- A coarse-grained protein model in a water-like solvent.Scientific reports · 2013Article
- Extended surfaces modulate hydrophobic interactions of neighboring solutes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Protein stability at a carbon nanotube interface.The Journal of chemical physics · 2011Article
- Assisted peptide folding by surface pattern recognition.Biophysical journal · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Experimental evidence suggests that proteins adsorbed to hydrophobic surfaces at low coverages are stabilized relative to the bulk. For larger coverages, proteins unfold and form beta-sheets. We performed computer simulations on model proteins and found that: 1), For weakly adsorbing surfaces, unfolded conformations lose more entropy upon adsorption than folded ones. 2), The melting temperature, both in the bulk and at surfaces, decreases with increasing protein concentration because of favorable interprotein interactions. 3), Proteins in the bulk show large unfolding free energy barriers; this barrier decreases at stronger adsorbing surfaces. We conjecture that typical experimental temperatures appear to be below the bulk melting temperature for a single protein, but above the melting temperature for concentrated protein solutions. Purely thermodynamic factors then explain protein stabilization on adsorption at low concentrations. However, both thermodynamic and kinetic factors are important at higher concentrations. Thus, proteins in the bulk do not denature with increasing concentration due to large kinetic barriers, even though the aggregated state is thermodynamically preferred. However, they readily unfold upon adsorption, with the surface acting as a heterogeneous catalyst. The thermal behavior of proteins adsorbed to hydrophobic surfaces thus appears to follow behavior independent of their chemical specificity.
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Registered trials
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