The analysis of the interaction between C60 and lysozyme provides general rules to identify the forces that govern the thermodynamics of binding between proteins and carbon nanoparticles. The main driving force of the binding are van der Waals interactions. Polar solvation and entropy, contributions that are often neglected, are strongly detrimental to the binding. These energetically relevant terms must be taken into account when protein/CNP hybrids are designed.
Calvaresi, M., Bottoni, A., Zerbetto, F. (2015). Thermodynamics of Binding Between Proteins and Carbon Nanoparticles: The Case of C60@Lysozyme. JOURNAL OF PHYSICAL CHEMISTRY. C, 119(50), 28077-28082 [10.1021/acs.jpcc.5b09985].
Thermodynamics of Binding Between Proteins and Carbon Nanoparticles: The Case of C60@Lysozyme
CALVARESI, MATTEO;BOTTONI, ANDREA;ZERBETTO, FRANCESCO
2015
Abstract
The analysis of the interaction between C60 and lysozyme provides general rules to identify the forces that govern the thermodynamics of binding between proteins and carbon nanoparticles. The main driving force of the binding are van der Waals interactions. Polar solvation and entropy, contributions that are often neglected, are strongly detrimental to the binding. These energetically relevant terms must be taken into account when protein/CNP hybrids are designed.| File | Dimensione | Formato | |
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J Phys Chem C Rev2.pdf
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