DNA hybridization sensors (3,4, 18). We have shown that bridization. the interaction between this short DNA molecule and the positively charged substrate is strong, as evidenced by the relatively small desorption rate constants and surface diffu-1 To whom correspondence should be addressed. sion co
Adsorption Mechanism of Polypeptides and Their Location at Hydrophobic Interfaces
✍ Scribed by Tobias Pirzer; Thorsten Hugel
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 398 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1439-4235
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
The adhesion of polypeptides and proteins at interfaces is important for a wide variety of systems—from the adhesion onto vessels during their production process over functional coatings to protein–membrane interactions in single cells. Herein, we apply an atomic‐force‐microscopy‐based single‐molecule method and poly‐D‐tyrosine to determine the adhesion strength and location of polypeptides at interfaces. Surprisingly, the support (solid, liquid or gas) hardly influences the adhesion in an aqueous environment, while the addition of ethanol to the solvent cuts the adhesion in half. These findings allow us to propose that the adsorbed polypeptide spans over both the depletion layer and the hydrophobic hydration layer to facilitate a compensation mechanism between dispersive and hydration forces.
📜 SIMILAR VOLUMES
tension (4,5). Standard free energy of adsorption for sur-Measurements of the surface tension of aqueous solutions of face-active solutes of aqueous solution at aqueous solutiondecylammonium chloride (DACl) and cesium perfluorooctanoate air (hydrocarbon) interfaces has been calculated by a num-(CsPF
Adsorption kinetic data recorded for \(\alpha\)-lactalbumin, \(\beta\)-casein, \(\beta\)-lactoglobulin, and bovine serum albumin at silanized silica surfaces of low and high hydrophobicity, along with the surfactant-mediated elutability of each from hydrophobic silica, were interpreted with referenc