Chemical composition and acid-base properties of the surface of GaAs-CdS solid solutions

Kirovskaya, I. A.; Zemtsov, A. E.

doi:10.1134/s0036024407010189

Cited by 2 publications

(2 citation statements)

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“…Moreover, Bergman et al observed that human serum albumin is preferentially adsorbed inside pits on GaAs substrates at pH 7.6 and the molecules appear to be packed closely together around the inner sides of rims that decorate the pits. Their results can also be understood in the context of our model; albumin has a negative net charge at pH 7.6, and the isoelectric point of GaAs is below pH 7.6 . Consequently, the substrate has a negative net surface charge at pH 7.6 and only dispersion interactions are attractive.…”

Section: Resultsmentioning

confidence: 58%

“…Their results can also be understood in the context of our model; albumin has a negative net charge at pH 7.6, 44 and the isoelectric point of GaAs is below pH 7.6. 45 Consequently, the substrate has a negative net surface charge at pH 7.6 and only dispersion interactions are attractive. According to the presented mechanism, such a configuration promotes adsorption only near the concave corners of the rims in equilibrium and allows the proteins to penetrate their electrostatic barrier for clustering.…”

Section: Resultsmentioning

confidence: 99%

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Electrostatic and Dispersion Interactions during Protein Adsorption on Topographic Nanostructures

2011

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Recently, biomaterials research has focused on developing functional implant surfaces with well-defined topographic nanostructures in order to influence protein adsorption and cellular behavior. To enhance our understanding of how proteins interact with such surfaces, we analyze the adsorption of lysozyme on an oppositely charged nanostructure using a computer simulation. We present an algorithm that combines simulated Brownian dynamics with numerical field calculation methods to predict the preferred adsorption sites for arbitrarily shaped substrates. Either proteins can be immobilized at their initial adsorption sites or surface diffusion can be considered. Interactions are analyzed on the basis of Derjaguin-Landau-Verway-Overbeek (DLVO) theory, including electrostatic and London dispersion forces, and numerical solutions are derived using the Poisson-Boltzmann and Hamaker equations. Our calculations show that for a grooved nanostructure (i.e., groove and plateau width 8 nm, height 4 nm), proteins first contact the substrate primarily near convex edges because of better geometric accessibility and increased electric field strengths. Subsequently, molecules migrate by surface diffusion into grooves and concave corners, where short-range dispersion interactions are maximized. In equilibrium, this mechanism leads to an increased surface protein concentration in the grooves, demonstrating that the total amount of protein per surface area can be increased if substrates have concave nanostructures.

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Section: Resultsmentioning

confidence: 58%

Section: Resultsmentioning

confidence: 99%