Mechanism Underlying Specificity of Proteins Targeting Inorganic Materials

Hayashi, T.; Sano, Ken‐Ichi; Shiba, Kiyotaka; Kumashiro, Yoshikazu; Iwahori, Keisuke; Yamashita, Ichiro; Hara, Masahiko

doi:10.1021/nl060050n

Cited by 118 publications

(131 citation statements)

References 33 publications

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“…[147] It was suggested that the speci-ficity of binding was due to electrostatic interactions between peptide and surface groups of the titanium substrate. [148] This N-terminal extension is uniquely presented on the exterior surface of the ferritin cage and is readily altered by genetic manipulation.…”

Section: Ferritin: Exteriormentioning

confidence: 99%

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Uchida¹,

Klem²,

Allen³

et al. 2007

Advanced Materials

536

518

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Materials scientists increasingly draw inspiration from the study of how biological systems fabricate materials under mild synthetic conditions by using self‐assembled macromolecular templates. Containerlike protein architectures such as viral capsids and ferritin are examples of such biological templates. These protein cages have three distinct interfaces that can be synthetically exploited: the interior, the exterior, and the interface between subunits. The subunits that comprise the building blocks of these structures can be modified both chemically and genetically in order to impart designed functionality to different surfaces of the cage. Therefore, the cages possess a great deal of synthetic flexibility, which allows for the introduction of multifunctionality in a single cage. In addition, hierarchical assembly of the functionalized cages paves the way for development of a new class of materials with a wide range of applications from electronics to biomedicine.

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Section: Ferritin: Exteriormentioning

confidence: 99%

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Uchida¹,

Klem²,

Allen³

et al. 2007

Advanced Materials

536

518

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“…Adsorption of protein on various materials has been widely studied and it has been found that factors such as electrostatic interaction, hydrophobic interaction, hydrogen bonding, VDW interaction and specific chemical interactions between protein and the adsorbent play important roles [56][57][58][59][60][61][62][63][64][65][66][67][68][69][70][71]. Short peptide sequences interact with TiO 2 surface via electrostatic interaction also [57][58][59].…”

Section: Adsorption Mechanism Of Rgdmentioning

confidence: 99%

Adsorption of tripeptide RGD on rutile TiO2 nanotopography surface in aqueous solution

et al. 2010

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“…7,8 Understanding water adsorption on TiO 2 is the key not only to efficiently split water molecules (as made use of in hydrogen gas production 9 ) but also to optimize adsorption on, and functionalization of, TiO 2 by larger molecules as mediated via strongly bound surface waters. [10][11][12][13][14][15] On the other hand, concerns have been raised with respect to environmental safety and health when TiO 2 is used in medical implants 16 and as engineered nanoparticles in consumer products. 17 TiO 2 nanoparticles are small enough to penetrate the blood-brain barrier, 18 can aggregate in organisms and the environment, and yield a nanotoxic response by increasing the levels of intracellular reactive oxygen species, leading to apoptosis.…”

Section: Introductionmentioning

confidence: 99%

Diffusion and reaction pathways of water near fully hydrated TiO2 surfaces from ab initio molecular dynamics

Agosta

Brandt

Lyubartsev

2017

The Journal of Chemical Physics

104

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Ab initio molecular dynamics simulations are reported for water-embedded TiO2 surfaces to determine the diffusive and reactive behavior at full hydration. A three-domain model is developed for six surfaces [rutile (110), (100), and (001), and anatase (101), (100), and (001)] which describes waters as “hard” (irreversibly bound to the surface), “soft” (with reduced mobility but orientation freedom near the surface), or “bulk.” The model explains previous experimental data and provides a detailed picture of water diffusion near TiO2 surfaces. Water reactivity is analyzed with a graph-theoretic approach that reveals a number of reaction pathways on TiO2 which occur at full hydration, in addition to direct water splitting. Hydronium (H3O+) is identified to be a key intermediate state, which facilitates water dissociation by proton hopping between intact and dissociated waters near the surfaces. These discoveries significantly improve the understanding of nanoscale water dynamics and reactivity at TiO2 interfaces under ambient conditions.

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Mechanism Underlying Specificity of Proteins Targeting Inorganic Materials

Cited by 118 publications

References 33 publications

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Adsorption of tripeptide RGD on rutile TiO2 nanotopography surface in aqueous solution

Diffusion and reaction pathways of water near fully hydrated TiO2 surfaces from ab initio molecular dynamics

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