The role of protein binding in the poisoning of gold nanoparticle catalysts

Chen, Yan; Flowers, Kaleyhia; Calizo, Milagros; Bishnoi, Sandra Whaley

doi:10.1016/j.colsurfb.2009.10.043

Cited by 8 publications

(6 citation statements)

References 43 publications

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“…When adding bovine serum albumin (BSA) as a known catalyst poison 29, a dramatic change is observed in the glucose oxidation current. Figure 6C (i) and (ii) show the current for glucose oxidation on bare gold nanoparticle catalyst before and after addition BSA (3 mg in 50 cm 3 solution), respectively.…”

Section: Resultsmentioning

confidence: 99%

Intrinsically Porous Polymer Protects Catalytic Gold Particles for Enzymeless Glucose Oxidation

et al. 2014

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The enzymeless glucose oxidation process readily occurs on nano‐gold electrocatalyst at pH 7, but it is highly susceptible to poisoning (competitive binding), for example from protein or chloride. Is it shown here that gold nanoparticle catalyst can be protected against poisoning by a polymer of intrinsic microporosity (PIM‐EA‐TB with BET surface area 1027 m2 g−1). This PIM material when protonated, achieves a triple catalyst protection effect by (i) size selective repulsion of larger protein molecules (albumins) and (ii) membrane ion selection effects, and (iii) membrane ion activity effects. PIM materials allow “environmental control” to be introduced in electrocatalytic processes.

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Section: Resultsmentioning

confidence: 99%

Intrinsically Porous Polymer Protects Catalytic Gold Particles for Enzymeless Glucose Oxidation

et al. 2014

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“…The high structure flexibility of BSA probably allowed easy refolding of the BSA molecule to adapt to the surface. A conformational change in BSA upon its adsorption onto the 2D surface or NPs has been well documented. ,,− The Au NPs were coated with citrate, and the Fe 3 O 4 NPs were stabilized with PAA . The longer chain of PAA than the citrate groups on the Au surface may extend the thickness of the diffusion layer and prevent the BSA molecules to get closer to the Fe 3 O 4 NPs surface.…”

Section: Resultsmentioning

confidence: 99%

“…However, low sensitivity, spectral interference from NPs in the background, requirement for protein or NP immobilization, and/or necessity for NPs to be luminescent or photoquenching prevent one from using the above techniques for studying NPs and proteins with wide ranges of physicochemical properties . Moreover, it is difficult for these techniques to probe the interaction-induced changes in protein’s binding capability to its ligands, substrates, or carrier molecules. ,,− …”

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confidence: 99%

Probing Nanoparticle−Protein Interaction by Capillary Electrophoresis

Zeng

et al. 2010

Anal. Chem.

100

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Understanding nanoparticle-protein interaction could help in promoting applications of nanoparticles in the biomedical fields and reducing/preventing possible adverse effects to the biological systems caused by nanoparticles. Quantitative measurement of the biophysical parameters of nanoparticle-protein interaction will improve such understanding, which could be conveniently performed by capillary electrophoresis (CE) as demonstrated in the present study. Two interaction situations were identified. Stable nanoparticle-protein complexes were resolved from the free nanoparticles and the proteins by capillary zone electrophoresis (CZE). Transient complexes with fast association/dissociation rates showed distinct mobility change from the free nanoparticles in affinity capillary electrophoresis (ACE). Interactions of bovine serum albumin (BSA) with the Fe(3)O(4) nanoparticles (average diameters of 8 and 10 nm) and with the Au nanoparticles (average diameters of 5 and 10 nm) displayed slow and fast binding kinetics, respectively. Using the Hill equation, we could calculate the dissociation constants (K(D)) and cooperativity coefficients (n). Impacts on nanoparticle-protein interaction from the physicochemical properties of nanoparticles and the incubation buffer were evaluated on the basis of the K(D) and n values to interpret the interaction driving forces. Our study demonstrated the high simplicity and flexibility of CE in probing the interaction of proteins with diverse particles. The separation power of CE should also facilitate studies of the multicomponent interaction systems for investigating how adsorption onto nanoparticles could affect the protein-protein or protein-small molecule interactions.

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“…Serum albumin protein is known to have a high affinity to gold surfaces, especially surfaces coated by citrates 9. Recently, it was reported that the presence of bovine serum albumin (BSA) largely affects the seed‐mediated growth of Au NPs, and thus hinders sensitive detection of H 2 O 2 10. Therefore, the change in SPR absorption during the gold‐growth reaction was examined at fixed concentrations of HAuCl 4 , H 2 O 2 , and Au@ h ‐SiO 2 nanospheres in the presence of different concentrations of BSA.…”

Section: Methodsmentioning

confidence: 99%