2008
DOI: 10.1016/j.biomaterials.2008.06.013
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Induced stepwise conformational change of human serum albumin on carbon nanotube surfaces

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Cited by 138 publications
(117 citation statements)
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References 51 publications
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“…For example, The oligopeptide, Arg-Gly-Asp (RGD) tripeptides, fibronectin and HSA adsorption behaviour on rutile (110) surface have been studied by MD based on the Amber force field [154,155] and the Charmm force field [156]. The conformational change of HSA in the process of adsorption on a carbon nanotube surface also is simulated by the MD method based on the Charmm force field [157]. The interactive behaviours between different subdomains of HSA and graphite surfaces with or without water [158,159], and adsorption behaviour of certain oligopeptides on quartz surfaces have been evaluated by MD based on the CVFF force field [160].…”
Section: Molecular Dynamics Simulation Of Protein Adsorptionmentioning
confidence: 99%
“…For example, The oligopeptide, Arg-Gly-Asp (RGD) tripeptides, fibronectin and HSA adsorption behaviour on rutile (110) surface have been studied by MD based on the Amber force field [154,155] and the Charmm force field [156]. The conformational change of HSA in the process of adsorption on a carbon nanotube surface also is simulated by the MD method based on the Charmm force field [157]. The interactive behaviours between different subdomains of HSA and graphite surfaces with or without water [158,159], and adsorption behaviour of certain oligopeptides on quartz surfaces have been evaluated by MD based on the CVFF force field [160].…”
Section: Molecular Dynamics Simulation Of Protein Adsorptionmentioning
confidence: 99%
“…[18][19][20] It takes into account the effects of important experimental conditions, such as temperature, pressure, and the aqueous environment. In addition, the adsorption dynamics of peptides/proteins on CNT surfaces, and the molecular-level interaction taking place between the peptides/proteins and the CNTs, as well as the local features (including secondary and tertiary structural changes, orientation and reorientation of proteins on the interface, hydrogen bonding, etc.)…”
Section: Introductionmentioning
confidence: 99%
“…Zhang et al [65] also reported that different types of functionalized multi-walled CNTs (MWCNTs) were able to bind to, or near to the catalytic site of the digestive enzyme α-chymotrypsin and inhibited its proteolytic activity completely. In a similar study it could be shown that the loss of activity was a function of the change in secondary structure upon adsorption of the proteins onto the surface of the SWCNTs [66,67]. On the other hand there are also studies that report that different metalloproteins immobilized on carboxylated SWCNTs did not show a detectable retention of their activity [68].…”
Section: Mechanism Of Interactionmentioning
confidence: 80%