Induced stepwise conformational change of human serum albumin on carbon nanotube surfaces

Shen, Jia-Wei; Wu, Tao; Wang, Qi; Kang, Yu

doi:10.1016/j.biomaterials.2008.06.013

Cited by 138 publications

(117 citation statements)

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%

A review of protein adsorption on bioceramics

et al. 2012

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Bioceramics, because of its excellent biocompatible and mechanical properties, has always been considered as the most promising materials for hard tissue repair. It is well know that an appropriate cellular response to bioceramics surfaces is essential for tissue regeneration and integration. As the in vivo implants, the implanted bioceramics are immediately coated with proteins from blood and body fluids, and it is through this coated layer that cells sense and respond to foreign implants. Hence, the adsorption of proteins is critical within the sequence of biological activities. However, the biological mechanisms of the interactions of bioceramics and proteins are still not well understood. In this review, we will recapitulate the recent studies on the bioceramic -protein interactions.

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Section: Molecular Dynamics Simulation Of Protein Adsorptionmentioning

confidence: 99%

A review of protein adsorption on bioceramics

et al. 2012

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“…[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%

Adsorption of Insulin Peptide on Charged Single‐Walled Carbon Nanotubes: Significant Role of Ordered Water Molecules

Shen

Wang

et al. 2009

ChemPhysChem

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Ordered hydration shells: The more ordered hydration shells outside the charged CNT surfaces prevent more compact adsorption of the peptide in the charged CNT systems [picture: see text], but peptide binding strengths on the charged CNT surfaces are stronger due to the electrostatic interaction.Studies of adsorption dynamics and stability for peptides/proteins on single-walled carbon nanotubes (SWNTs) are of great importance for a better understanding of the properties and nature of nanotube-based biosystems. Herein, the dynamics and mechanism of the adsorption of the insulin chain B peptide on different charged SWNTs are investigated by explicit solvent molecular dynamics simulations. The results show that all types of surfaces effectively attract the model peptide. Water molecules play a significant role in peptide adsorption on the surfaces of charged carbon nanotubes (CNTs). Compared to peptide adsorption on neutral CNT surfaces, the more ordered hydration shells outside the tube prevent more compact adsorption of the peptide in charged CNT systems. This shield effect leads to a smaller conformational change and van der Waals interaction between the peptide and surfaces, but peptide binding strengths on charged CNT surfaces are stronger than those on the neutral CNT surface due to the strong electrostatic interaction. The result of these simulations implies the possibility of improving the binding strength of peptides/proteins on CNT surfaces, as well as keeping the integrity of the peptide/protein conformation in peptide/protein-CNT complexes by charging the CNTs.

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“…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%

The Role of the Protein Corona in Fiber Structure-Activity Relationships

Kucki

Kaiser

Clift

et al. 2014

Fibers

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When nanomaterials enter biological fluids, they are immediately covered by biomolecules, particularly proteins, forming the so-called protein corona. The dynamic nature and complexity of the protein corona can impact upon the biological effects and distribution of nanomaterials with an organism. Therefore, the protein corona is an important factor in determining the biological impact of any nanomaterials. The protein adsorption pattern is determined by various factors, including the bio-fluids' protein composition, the nanomaterials' physicochemical properties, as well as the time and type of exposure. Predominantly, research has focused upon spherical nano-objects, however, due to their ever-increasing potential use within human based applications, and, therefore, heightening and inevitable exposure to the human body, little is known regarding how proteins interact with nanofibers. Therefore, the present review focuses on the current knowledge as to how the geometry of man-made (nano)fibers, carbon nanotubes (in comparison with asbestos fibers), affects their interaction with proteins within biological fluids. Summarizing state-of the art methodologies applied to dissect protein-binding signatures, it is further discussed whether the protein corona composition of fibrous and OPEN ACCESSFibers 2014, 2 188 non-fibrous materials differ, as well as what impact the protein corona has on (nano)fiber uptake, intracellular distribution and their subsequent toxicity.

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Induced stepwise conformational change of human serum albumin on carbon nanotube surfaces

Cited by 138 publications

References 51 publications

A review of protein adsorption on bioceramics

A review of protein adsorption on bioceramics

Adsorption of Insulin Peptide on Charged Single‐Walled Carbon Nanotubes: Significant Role of Ordered Water Molecules

The Role of the Protein Corona in Fiber Structure-Activity Relationships

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