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Interaction of gold nanoparticles with protein: A spectroscopic study to monitor protein conformational changes
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View: Figures


Image of FIG. 1.
FIG. 1.

Reaction scheme of reduction of tetrachloroauric acid with glutamic acid and subsequent bioconjugation with BSA via electrostatic interactions. The inset shows the transfer of energy from the tryptophan residue of BSA (donor) to GNPs (acceptor) where GNPs behave as excited state quenchers.

Image of FIG. 2.
FIG. 2.

Absorption spectra of GNP solution showing a surface plasmon peak at . The inset shows the picture of a glass vial containing monodispersed cherry-red colored GNPs. The relative surface plasmon resonance intensity of the GNPs was measured spectrophotometrically between 400 and . The corresponding TEM image of the sample is shown on the right side.

Image of FIG. 3.
FIG. 3.

Standard curve of fluorescence intensity vs FITC-BSA concentration. The inset shows the number of BSA per GNPs with respect to the concentration of BSA. The number of particles of gold and protein was calculated from their respective molarities.

Image of FIG. 4.
FIG. 4.

Effect of conjugation of GNPs on fluorescence intensity of tryptophan residue in BSA at 7.0. The concentrations of GNPs are a) 0, b) , (c) , (d) , (e) , and (f) .

Image of FIG. 5.
FIG. 5.

CD spectra of native BSA (curve a) and BSA conjugated with different concentrations of GNPs (curves b–f) at pH 7.0. Inset shows the plot of corresponding mean residual ellipticity (MRE) at vs the concentration of GNPs.


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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Interaction of gold nanoparticles with protein: A spectroscopic study to monitor protein conformational changes