2014
DOI: 10.1021/nn4063374
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Abstract: Integrating carbon nanoparticles (CNPs) with proteins to form hybrid functional assemblies is an innovative research area with great promise for medical, nanotechnology, and materials science. The comprehension of CNP-protein interactions requires the still-missing identification and characterization of the 'binding pocket' for the CNPs. Here, using Lysozyme and C60 as model systems and NMR chemical shift perturbation analysis, a protein-CNP binding pocket is identified unambiguously in solution and the effect… Show more

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Cited by 73 publications
(117 citation statements)
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“…[156][157][158] Two other (vibrational) spectroscopic methods to detect protein binding on a NP surface by investigating the vibration modes are Fourier transform infrared (FTIR) and Raman spectroscopy. NMR can provide high-resolution information on protein structural changes in biomolecule-NP complexes in aqueous solution, i.e.…”
Section: View Article Onlinementioning
confidence: 99%
“…[156][157][158] Two other (vibrational) spectroscopic methods to detect protein binding on a NP surface by investigating the vibration modes are Fourier transform infrared (FTIR) and Raman spectroscopy. NMR can provide high-resolution information on protein structural changes in biomolecule-NP complexes in aqueous solution, i.e.…”
Section: View Article Onlinementioning
confidence: 99%
“…As shown in Fig. 4, a superposition of 2D 1 H, 15 N HSQC spectrum of free lysozyme (LSZ) and C 60 @LSZ hybrid can be used to determine the NH group of the protein backbone (Calvaresi et al 2014). Only a few NH backbone groups undergo significant change in chemical shift upon binding to C 60 , with the majority of them remaining unaffected, which indicates that the interaction of C 60 with LSZ is very specific and affects only a few amino acids.…”
Section: Binding Sitesmentioning
confidence: 99%
“…101 Furthermore, according to the nest's size, proteins are able to selectively bind the fullerene cage whose size satisfies the perfect protein-GNMs shape-complementarity. 104 They were able to distinctively determine the adsorption of fullerene onto the protein surface by UV-vis measurements, and the imperceptible variation in the circular dichroism (CD) plot demonstrates the structural stability of the protein upon binding. 102 The peculiar hydrophobic and vdW nature of binding that characterize fullerene-proteins interaction are indeed the ideal conditions in which the 55% rule holds, prompting that might efficiently describe this hybrid complexation.…”
Section: Fullerenes and Proteinsmentioning
confidence: 99%