ArticleProceedings of the National Academy of Sciences of the United States of America2000
Peptide interfacial adsorption is kinetically limited by the thermodynamic stability of self association.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Emerging Emulsifiers: Conceptual Basis for the Identification and Rational Design of Peptides with Surface Activity.International journal of molecular sciences · 2021Review
- Using elongated microparticles to enhance tailorable nanoemulsion delivery in excised human skin and volunteers.Journal of controlled release : official journal of the Controlled Release Society · 2018Article
- Dynamic surface tension and adsorption mechanism of surfactin biosurfactant at the air-water interface.European biophysics journal : EBJ · 2018Article
- Computational study of elements of stability of a four-helix bundle protein biosurfactant.Journal of computer-aided molecular design · 2015Article
- Insights into the role of protein molecule size and structure on interfacial properties using designed sequences.Journal of the Royal Society, Interface · 2013Article
- A kinetic model for beta-amyloid adsorption at the air/solution interface and its implication to the beta-amyloid aggregation process.The journal of physical chemistry. B · 2009Article
- The interfacial structure and Young's modulus of peptide films having switchable mechanical properties.Journal of the Royal Society, Interface · 2008Article
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Authors and funding
3 authors.
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Abstract
We present a study of the adsorption of two peptides at the octane-water interface. The first peptide, Lac21, exists in mixed monomer-tetramer equilibrium in bulk solution with an appreciable monomer concentration. The second peptide, Lac28, exists as a tetramer in solution, with minimal exposed hydrophobic surface. A kinetic limitation to interfacial adsorption exists for Lac28 at moderate to high surface coverage that is not observed for Lac21. We estimate the potential energy barrier for Lac28 adsorption to be 42 kJ/mol and show that this is comparable to the expected free energy barrier for tetramer dissociation. This finding suggests that, at moderate to high surface coverage, adsorption is kinetically limited by the availability of interfacially active monomeric "domains" in the subinterfacial region. We also show how the commonly used empirical equation for protein adsorption dynamics can be used to estimate the potential energy barrier for adsorption. Such an approach is shown to be consistent with a formal description of diffusion-adsorption, provided a large potential energy barrier exists. This work demonstrates that the dynamics of interfacial adsorption depend on protein thermodynamic stability, and hence structure, in a quantifiable way.
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