ArticleBiophysical journal2008
An entropic perspective of protein stability on surfaces.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Mining peptides for mining solutions: evaluation of calcium-binding peptides for rare earth element separations.Chemical science · 2025Article
- Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles.The journal of physical chemistry. B · 2023Article
- Structural preferences shape the entropic force of disordered protein ensembles.bioRxiv : the preprint server for biology · 2023Article
- Multifunctional synthetic nano-chaperone for peptide folding and intracellular delivery.Nature communications · 2022Article
- Exploring Glycan Binding Specificity of Odorranalectin by Alanine Scanning Library.European journal of organic chemistry · 2022Article
- The effect of charged residue substitutions on the thermodynamics of protein-surface interactions.Protein science : a publication of the Protein Society · 2021Article
- Directed Evolution Using Stabilized Bacterial Peptide Display.Journal of the American Chemical Society · 2020Article
- Surface Attachment Enhances the Thermodynamic Stability of Protein L.Angewandte Chemie (International ed. in English) · 2019Article
- Experimental Measurement of Surface Charge Effects on the Stability of a Surface-Bound Biopolymer.Langmuir : the ACS journal of surfaces and colloids · 2018Article
- Structural studies unravel the active conformation of apo RORγt nuclear receptor and a common inverse agonism of two diverse classes of RORγt inhibitors.The Journal of biological chemistry · 2017Article
- The effects of tether placement on antibody stability on surfaces.The Journal of chemical physics · 2017Article
- Entropic and electrostatic effects on the folding free energy of a surface-attached biomolecule: an experimental and theoretical study.Journal of the American Chemical Society · 2012Article
- Permeability of anti-fouling PEGylated surfaces probed by fluorescence correlation spectroscopy.Colloids and surfaces. B, Biointerfaces · 2011Article
- Protein stability at a carbon nanotube interface.The Journal of chemical physics · 2011Article
- Migration of marrow stromal cells in response to sustained release of stromal-derived factor-1alpha from poly(lactide ethylene oxide fumarate) hydrogels.International journal of pharmaceutics · 2010Article
- Release characteristics and osteogenic activity of recombinant human bone morphogenetic protein-2 grafted to novel self-assembled poly(lactide-co-glycolide fumarate) nanoparticles.Journal of controlled release : official journal of the Controlled Release Society · 2009Article
- Salt effects on surface-tethered peptides in solution.The journal of physical chemistry. B · 2009Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The interaction of proteins with surfaces regulates numerous processes in nature, science, and technology. In many applications, it is desirable to place proteins on surfaces in an active state, and tethering represents one manner in which to accomplish this. However, a clear understanding of how tether placement and design affects protein activity is lacking. Available theoretical models predict that proteins will be stabilized when tethered to substrates. Such models suggest that the surface reduces the number of states accessible to the unfolded state of the protein, thereby reducing the entropic cost of folding on the surface compared to the bulk case. Recent studies, however, have shown that this stabilization is not always seen. The purpose of this article is to determine the validity of the theory with a thorough thermodynamic analysis of the folding of peptides attached to surfaces. Configuration-temperature-density-of-states Monte Carlo simulations are used to examine the behavior of four different peptides of different secondary and tertiary structure. It is found that the surface does reduce the entropic cost of folding for tethered peptides, as the theory suggests. This effect, however, does not always translate into improved stability because the surface may also have a destabilizing enthalpic effect. The theory neglects this effect and assumes that the enthalpy of folding is the same on and off the surface. Both the enthalpic and entropic contributions to the stability are found to be topology- and tether-placement-specific; we show that stability cannot be predicted a priori. A detailed analysis of the folding of protein A shows how the same protein can be both stabilized and destabilized on a surface depending upon how the tethering enhances or hinders the ability of the peptide to form correct tertiary structures.
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Registered trials
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