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.
Thermodynamics of Binding Between Proteins and Carbon Nanoparticles: The Case of C60@Lysozyme / Calvaresi, Matteo; Bottoni, Andrea; Zerbetto, Francesco. - In: JOURNAL OF PHYSICAL CHEMISTRY. C. - ISSN 1932-7447. - STAMPA. - 119:50(2015), pp. 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 | |
|---|---|---|---|
|
jp5b09985_si_001.pdf
accesso aperto
Tipo:
File Supplementare
Licenza:
Licenza per Accesso Aperto. Altra tipologia di licenza compatibile con Open Access
Dimensione
1.4 MB
Formato
Adobe PDF
|
1.4 MB | Adobe PDF | Visualizza/Apri |
|
J Phys Chem C Rev2.pdf
Open Access dal 19/11/2016
Tipo:
Postprint
Licenza:
Licenza per accesso libero gratuito
Dimensione
798.57 kB
Formato
Adobe PDF
|
798.57 kB | Adobe PDF | Visualizza/Apri |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
