Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations
Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations
Lin ZHANG1,2, Yan SUN1,2()
1. Department of Biochemical Engineering and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300072, China; 2. Collaborative Innovation Center of Chemical Science and Engineering (Tianjin), Tianjin 300072, China
Hydrophobic charge induction chromatography (HCIC) is a mixed-mode chromatography which is advantageous for high adsorption capacity and facile elution. The effect of the ligand chain length on protein behavior in HCIC was studied. A coarse-grain adsorbent pore model established in an earlier work was modified to construct adsorbents with different chain lengths, including one with shorter ligands (CL2) and one with longer ligands (CL4). The adsorption, desorption, and conformational transition of the proteins with CL2 and CL4 were examined using molecular dynamics simulations. The ligand chain length has a significant effect on both the probability and the irreversibility of the adsorption/desorption. Longer ligands reduced the energy barrier of adsorption, leading to stronger and more irreversible adsorption, as well as a little more unfolding of the protein. The simulation results elucidated the effect of the ligand chain length, which is beneficial for the rational design of adsorbents and parameter optimization for high-performance HCIC.
Corresponding Author(s):
SUN Yan,Email:ysun@tju.edu.cn
引用本文:
. Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations[J]. Frontiers of Chemical Science and Engineering, 2013, 7(4): 456-463.
Lin ZHANG, Yan SUN. Effect of ligand chain length on hydrophobic charge induction chromatography revealed by molecular dynamics simulations. Front Chem Sci Eng, 2013, 7(4): 456-463.
Adsorbent pore with shorter ligand containing two beads each
CL4
Adsorbent pore with longer ligand containing four beads each
d
The minimum distance between the protein and ligand
D
Desorbed state of protein
E
Inter-molecular interaction energy between protein and ligand
f
Mole fraction
M
Intermediate state of protein
N
Native state of protein
PB
Adsorption probability
PD
Desorption probability
Rg
Radius of gyration of protein
U
Unfolded state of protein
YB
Adsorption irreversibility
YD
Desorption irreversibility
χ
Structural overlap function
Tab.2
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