Adsorption and Orientation of the Physiological Extracellular Peptide Glutathione Disulfide on Surface Functionalized Colloidal Alumina Particles

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• 作者：Fabian Meder ; Henrik Hintz ; Yvonne Koehler ; Maike M. Schmidt ; Laura Treccani ; Ralf Dringen ; Kurosch Rezwan
• 刊名：The Journal of the American Chemical Society
• 出版年：2013
• 出版时间：April 24, 2013
• 年：2013
• 卷：135
• 期：16
• 页码：6307-6316
• 全文大小：503K
• 年卷期：v.135,no.16(April 24, 2013)
• ISSN：1520-5126

文摘

Understanding the interrelation between surface chemistry of colloidal particles and surface adsorption of biomolecules is a crucial prerequisite for the design of materials for biotechnological and nanomedical applications. Here, we elucidate how tailoring the surface chemistry of colloidal alumina particles (d₅₀ = 180 nm) with amino (鈭扤H₂), carboxylate (鈭扖OOH), phosphate (鈭扨O₃H₂) or sulfonate (鈭扴O₃H) groups affects adsorption and orientation of the model peptide glutathione disulfide (GSSG). GSSG adsorbed on native, 鈭扤H₂-functionalized, and 鈭扴O₃H-functionalized alumina but not on 鈭扖OOH- and 鈭扨O₃H₂-functionalized particles. When adsorption occurred, the process was rapid (鈮? min), reversible by application of salts, and followed a Langmuir adsorption isotherm dependent on the particle surface functionalization and 味 potential. The orientation of particle bound GSSG was assessed by the release of glutathione after reducing the GSSG disulfide bond and by 味 potential measurements. GSSG is likely to bind via the carboxylate groups of one of its two glutathionyl (GS) moieties onto native and 鈭扤H₂-modified alumina, whereas GSSG is suggested to bind to 鈭扴O₃H-modified alumina via the primary amino groups of both GS moieties. Thus, GSSG adsorption and orientation can be tailored by varying the molecular composition of the particle surface, demonstrating a step toward guiding interactions of biomolecules with colloidal particles.