Please use this identifier to cite or link to this item: https://doi.org/5/055308
Title: A thermodynamic study of peptides binding to carbon nanotubes based on a hydrophobic-polar lattice model using Monte Carlo simulations
Authors: Cheng, Y.
Liu, G.R. 
Li, Z.R.
Lu, C.
Mi, D.
Issue Date: 7-Mar-2008
Source: Cheng, Y.,Liu, G.R.,Li, Z.R.,Lu, C.,Mi, D. (2008-03-07). A thermodynamic study of peptides binding to carbon nanotubes based on a hydrophobic-polar lattice model using Monte Carlo simulations. Journal of Physics D: Applied Physics 41 (5) : -. ScholarBank@NUS Repository. https://doi.org/5/055308
Abstract: Carbon nanotubes (CNTs) are outstanding novel materials that have great potential for a variety of chemical and biomedical applications. However, the mechanism of their interactions with biomaterials is still not fully understood, and more insightful research work is needed. In this work, we use the 2D hydrophobic-polar lattice model and the Monte Carlo simulation method to study the interactions between model peptides and CNTs. The energy parameters of the coarse-grained lattice model are qualitatively determined based on experimental data and molecular dynamics simulation results. Our model is capable of reproducing the essential phenomena of peptides folding in bulk water and binding to CNTs, as well as providing new insights into the thermodynamics and conformational properties of peptides interacting with nanotubes. The results suggest that both the internal energy and the peptide conformational entropy contribute to the binding process. Upon binding to the CNTs, peptides generally unfold into their denatured structures before they reach the lowest-accessible energy states of the system. Temperature has a significant influence on the adsorption process. © 2008 IOP Publishing Ltd.
Source Title: Journal of Physics D: Applied Physics
URI: http://scholarbank.nus.edu.sg/handle/10635/59310
ISSN: 00223727
DOI: 5/055308
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