TY - JOUR
T1 - A thermodynamic study of peptides binding to carbon nanotubes based on a hydrophobic-polar lattice model using Monte Carlo simulations
AU - Cheng, Y.
AU - Liu, G. R.
AU - Li, Z. R.
AU - Lu, C.
AU - Mi, D.
PY - 2008/3/7
Y1 - 2008/3/7
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=42549085256&partnerID=8YFLogxK
U2 - 10.1088/0022-3727/41/5/055308
DO - 10.1088/0022-3727/41/5/055308
M3 - Article
AN - SCOPUS:42549085256
SN - 0022-3727
VL - 41
JO - Journal of Physics D: Applied Physics
JF - Journal of Physics D: Applied Physics
IS - 5
M1 - 055308
ER -