ArticleThe Journal of chemical physics2011
Protein stability at a carbon nanotube interface.
Article in The Journal of chemical physics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Enzyme immobilization studied through molecular dynamic simulations.Frontiers in bioengineering and biotechnology · 2023Review
- A Possible Mechanism of Graphene Oxide to Enhance Thermostability of D-Psicose 3-Epimerase Revealed by Molecular Dynamics Simulations.International journal of molecular sciences · 2021Article
- The unpredictable carbon nanotube biocorona and a functionalization method to prevent protein biofouling.Journal of nanobiotechnology · 2021Article
- Atomic Details of Carbon-Based Nanomolecules Interacting with Proteins.Molecules (Basel, Switzerland) · 2020Review
- Comparison of Attachment and Antibacterial Activity of Covalent and Noncovalent Lysozyme-Functionalized Single-Walled Carbon Nanotubes.ACS omega · 2020Article
- Protein-Nanoparticle Interaction: Corona Formation and Conformational Changes in Proteins on Nanoparticles.International journal of nanomedicine · 2020Review
- Multi-walled carbon nanotubes increase antibody-producing B cells in mice immunized with a tetravalent vaccine candidate for dengue virus.Journal of nanobiotechnology · 2016Article
- Immobilization of glucose oxidase to nanostructured films of polystyrene-block-poly(2-vinylpyridine).Journal of colloid and interface science · 2014Article
- Formation and cell translocation of carbon nanotube-fibrinogen protein corona.Applied physics letters · 2012Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interactions of proteins with solid surfaces occur in a variety of situations. Motivated by the many nanoengineering applications of protein-carbon nanotube hybrids, we investigate the conformational transitions of hen egg white lysozyme adsorbed on a carbon nanotube. Using a C(α) structure-based model and replica exchange molecular dynamics, we show how the folding/unfolding equilibrium of the adsorbed protein varies with the strength of its coupling to the surface. The stability of the native state depends on the balance between the favorable entropy and unfavorable enthalpy change on adsorption. In the case of a weakly attractive surface when the former dominates, the protein is stabilized. In this regime, the protein can fold and unfold while maintaining the same binding fraction. With increasing surface attraction, the unfavorable enthalpic effect dominates, the native state is destabilized, and the protein has to extensively unbind before changing states from unfolded to folded. At the highest surface coupling, the entropic penalty of folding vanishes, and a folding intermediate is strongly stabilized. In this intermediate state, the α-domain of lysozyme is disrupted, while the β-sheet remains fully structured. We rationalize the relative stability of the two domains on the basis of the residue contact order.
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