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Chapter 6 – Production of Few Layer Graphene in Aqueous Media for Biological Studies HSA has one Trp residue in subdomain IIA and 18 Tyr residues distributed throughout the protein at distances short enough for mutual Tyr → Tyr or Tyr → Trp FRET but, due to the lack of spectral overlap between Trp emission and Tyr absorption, Trp → Tyr energy transfer is unlikely.403 Hence, the dominant emission (~340 nm) in the fluorescence spectra excited at 280 nm (which is the absorption maximum of HSA, Figure 6.12c) is from Trp, with some contribution from Tyr (~310 nm).403, 428 Tyr does not contribute to the emission at longer wavelength excitation (295 nm), when selective Trp interactions could be investigated at this wavelength.403, 428 Figure 6.17: Fluorescence spectra of HSA-Control, G/HSA and G/HSA-wash, excited at 280 nm (a) and 295 nm (b) respectively. Samples were 10 fold diluted. The fluorescence emission spectra (300 nm - 500 nm region) of the control HSA and as-produced G/HSA excited at 280 nm and 295 nm are shown in Figure 6.17a and Figure 6.17b, respectively. The quenching of Tyr and Trp fluorescence in G/HSA was clearly observed compared to HSA control, due to its interaction with the graphene surface. Complete fluorescence quenching of Tyr and Trp was observed for G/HSA-wash, indicating the observed fluorescence of G/HSA is from the excess HSA present in the dispersion (~2.6 mg/ml excess HSA as estimated by Ninhydrin assay). These observations show that Tyr and Trp, which are the hydrophobic regions of HSA, are indeed interacting with graphene, presumably then responsible for enhancing the stability of the dispersion. Theoretical studies have shown that Tyr and Trp amino acids can be strongly adsorbed on graphene surfaces via 𝜋 → 𝜋 interactions.234 Unlike GO which has several groups attached to its surface,167 G/HSA comprised pristine FLG (no significant Raman D 189PDF Image | PRODUCTION AND APPLICATIONS OF GRAPHENE AND ITS COMPOSITES
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