Adsorption mechanism of BMP-7 on hydroxyapatite (001) surfaces

Zhou, Hailong; Wu, Tao; Dong, Xiuli; Wang, Qi; Shen, Jia-Wei

doi:10.1016/j.bbrc.2007.06.169

Cited by 108 publications

(80 citation statements)

References 27 publications

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“…Long-time and multiple MD simulations could overcome these drawbacks. However, herein, the model peptide contains only 30 amino acids, and our previous studies [20,[27][28][29] have shown that all-atom simulations of adsorption of protein or peptides with similar size on various surfaces could still provide efficient and useful information for the meta-stable structures in nanosecond scale. The time-dependent interaction energy, E int (t) for all the systems in MD simulations are defined by Equation (1):…”

Section: Modelling and Simulationsmentioning

confidence: 98%

“…[23,24] In addition, doping the nanotube would cause the electrons transferring from the n-type dopants to the SWNTs [25] or from SWNTs to p-type dopants. [26] In our previous studies, [20,[27][28][29] the dynamics of protein adsorption and desorption, as well as the protein-CNT interactions are varied in different material surfaces, for example, in hydrophilic hydroxyapatite surfaces and in hydrophobic SWNT surfaces. These studies indicate that the dynamics of the peptide/protein adsorption and the interaction between the peptide/protein and the material surfaces could be controlled by the properties and the textures of the material surfaces.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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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Section: Modelling and Simulationsmentioning

confidence: 98%

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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“…The chemical nature of the surface can induce greater protein-surface interactions through either electrostatic or hydrophobic interactions [104]. It is generally accepted that electrostatic force played a vital role in the protein adsorption process and has been proved by lots of experimental and computer simulation studies [98,[105][106][107] ) on HA is far different from that on OCP (figure 3). The same story also happened on other Ca-P.…”

Section: Protein Adsorption On Ca-p Ceramicsmentioning

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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“…Physical properties of polycrystalline materials strongly depend on the distribution of the crystallographic orientations of the surface grains [2]. Hydroxyapatite is the predominant inorganic component of human bones and teeth [6]. It has received much attention in materials science and medical fields because of its special surface interaction properties and biocompatibility [7,8].…”

Section: Introductionmentioning

confidence: 99%

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

Richert¹,

Boukari²,

Berner³

et al. 2011

JBNB

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The interaction of proteins with solid surfaces is a fundamental phenomenon in the biomaterials field. We investigated, using atomic force microscopy (AFM), the interactions of a recombinant amelogenin with titanium, a biphasic calcium phosphate (BCP) and mica. The unbinding processes were compared to those of an earlier studied protein, namely fibrinogen. Force spectroscopy (AFM) experiments were carried out at 0 ms, 10 2 ms, 10 3 ms and 10 4 ms of contact time. In general, the rupture forces increased as a function of interaction time. The unbinding forces of amelogenin interacting with the BCP surface were always stronger than those of the amelogenin-titanium system. The unbinding forces of fibrinogen interacting with the BCP surface were always much stronger than those of the fibrinogen-titanium system.For the most part, this study provides direct evidence that recombinant amelogenin binds more strongly than fibrinogen on the studied substrates.

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Adsorption mechanism of BMP-7 on hydroxyapatite (001) surfaces

Cited by 108 publications

References 27 publications

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

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

A review of protein adsorption on bioceramics

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

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