Pressure-induced protein adsorption at aqueous-solid interfaces
There seems to be a general relation between the standard Gibbs energy change of unfolding, ΔG°unf, of a protein and its affinity to aqueous-solid interfaces. So-called "hard" proteins (ΔG°unf is large) are found to adsorb less strongly to such interfaces than "soft" proteins (ΔG...
| Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 29(2013), 25 vom: 25. Juni, Seite 8025-30 |
|---|---|
| Auteur principal: | |
| Autres auteurs: | , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2013
|
| Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't Proteins |
| Résumé: | There seems to be a general relation between the standard Gibbs energy change of unfolding, ΔG°unf, of a protein and its affinity to aqueous-solid interfaces. So-called "hard" proteins (ΔG°unf is large) are found to adsorb less strongly to such interfaces than "soft" proteins (ΔG°unf is small). Here, we provide direct support for this rule by using high pressure to modulate the folding stability of a protein. We have performed high-pressure total internal reflection fluorescence (HP-TIRF) spectroscopy and high-pressure neutron reflectometry (HP-NR) to measure the degree of adsorption and the structure of lysozyme on planar solid surfaces as a function of pressure for the first time. By carrying out these experiments at hydrophilic and hydrophobic surfaces with varying concentrations of glycerol, we have found strong evidence that ΔG°unf has indeed a direct influence. At high pressures, there is a larger degree of lysozyme adsorption, probably because lysozyme becomes a "soft" protein under these conditions. The results of this study demonstrate that high pressure is a very useful tool to explore thermodynamics of protein-interface interactions |
|---|---|
| Description: | Date Completed 03.02.2014 Date Revised 29.08.2013 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la401296f |