AI Article Synopsis
- The study investigates how AFGP 8 proteins adhere to mica, revealing a strong affinity for hydrophilic surfaces.
- As protein concentration increases, different structural formations occur, leading to the development of single-molecule-high aggregates at low concentrations and larger 3-D aggregates at higher concentrations.
- The protein's hydrophilicity is evidenced by its ability to adsorb spontaneously from the solution, which was tracked through in situ imaging techniques.
Article Abstract
The adsorption of AFGP 8 on mica was studied by atomic force microscopy. The results shown in this paper emphasize the strong adsorption affinity of these proteins to hydrophilic surfaces, in this case mica. The dependence of the surface morphology while drying a droplet of protein solution, and the tendency to form 3-D aggregates at high concentration was observed. The behavior indicates that single-molecule-high aggregates (8.1 Å) are formed at low concentration; as the concentration increases, a double layer seems to appear in equilibrium with large aggregates; and as the concentration is increased further, the equilibrium is shifted toward larger aggregates leaving behind residual single-molecule-high aggregates. The hydrophilicity of the protein was demonstrated by the spontaneous adsorption of the protein directly from solution, as monitored by in situ imaging.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.colsurfb.2010.08.029 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!