4.8 Article

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

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 135, Issue 16, Pages 6307-6316

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/ja401590c

Keywords

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Funding

  1. EuropeanResearch Council within the BiocerEng [205509]
  2. European Research Council (ERC) [205509] Funding Source: European Research Council (ERC)

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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 (d(50) = 180 nm) with amino (-NH2), carboxylate (-COOH), phosphate (-PO3H2) or sulfonate (-SO3H) groups affects adsorption and orientation of the model peptide glutathione disulfide (GSSG). GSSG adsorbed on native, -NH2-functionalized, and -SO3H-functionalized alumina but not on -COOH- and -PO3H2-functionalized particles. When adsorption occurred, the process was rapid (<= 5 min), reversible by application of salts, and followed a Langmuir adsorption isotherm dependent on the particle surface functionalization and zeta potential. The orientation of particle bound GSSG was assessed by the release of glutathione after reducing the GSSG disulfide bond and by zeta potential measurements. GSSG is likely to bind via the carboxylate groups of one of its two glutathionyl (GS) moieties onto native and -NH2-modified alumina, whereas GSSG is suggested to bind to -SO3H-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.

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