Endowing a Ferritin‐Like Cage Protein with High Affinity and Selectivity for Certain Inorganic Materials

Sano, Ken‐Ichi; Ajima, Kumiko; Iwahori, Keisuke; Yudasaka, Masako; Iijima, Sumio; Yamashita, Ichiro; Shiba, Kiyotaka

doi:10.1002/smll.200500010

Cited by 118 publications

(119 citation statements)

References 52 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

530

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

530

518

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“…This is not the first time that such a pattern of binding behavior has been observed 50 for titania binding peptides: in addition, in this prior study, the authors were unable to account for the trend in binding behavior. 50 Figure 2, Table 3, and Table S1 in the Supporting Information provide further insight into the difference in adsorption and desorption behavior of the two peptides under the two solution conditions used for the binding experiments. Differences in the amount of surface-bound mass (even allowing for the fact that QCM measures the mass of liquid and ions adsorbed as well as the analyte (the peptide in this study)) as well as the rates of adsorption and desorption (Table S1) were measured.…”

Section: Qcm Binding Analysismentioning

confidence: 99%

Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Sultan

Westcott

Hughes

et al. 2016

ACS Appl. Mater. Interfaces

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A major barrier to the systematic improvement of biomimetic peptide-mediated strategies for the controlled growth of inorganic nanomaterials in environmentally benign conditions lies in the lack of clear conceptual connections between the sequence of the peptide and its surface binding affinity, with binding being facilitated by non-covalent interactions. Peptide conformation, both in the adsorbed and non-adsorbed state, is the key relationship that connects peptide-materials binding with peptide sequence. Here, we combine experimental peptide-titania binding characterization with state-of-the-art conformational sampling via molecular simulations to elucidate these structure/binding relationships for two very different titania-binding peptide sequences. The two sequences (Ti-1: QPYLFATDSLIK and Ti-2:GHTHYHAVRTQT) differ in their overall hydropathy, yet via quartz-crystal microbalance measurements and predictions from molecular simulations, we show these sequences both support very similar, strong titania-binding affinities. Our molecular simulations reveal that the two sequences exhibit profoundly different modes of surface binding, with Ti-1 acting as an entropically-driven binder while Ti-2 behaves as an enthalpically-driven binder. The integrated approach presented here provides a rational basis for peptide sequence engineering to achieve the in-situ growth and organization of titania nanostructures in aqueous media and for the design of sequences suitable for a range of technological applications that involve the interface between titania and biomolecules.3

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“…Furthermore, it was also demonstrated that accretion of surfactant reduced nonspecific interactions, dramatically enhancing the selectivity and specificity of this Ti-binding peptide (Sano et al, 2005a;2005b; (Rodahl et al,1996;Miyachi et al, 2000). The results of this study revealed a clear difference in frequency shift among the conditions set, indicating that the QCM-D technique is effective in the evaluation of adsorption behavior of peptides, including surfactants.…”

mentioning

confidence: 58%

Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides

et al. 2010

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Endowing a Ferritin‐Like Cage Protein with High Affinity and Selectivity for Certain Inorganic Materials

Cited by 118 publications

References 52 publications

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides

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Endowing a Ferritin‐Like Cage Protein with High Affinity and Selectivity for Certain Inorganic Materials

Cited by 118 publications

References 52 publications

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Biological Containers: Protein Cages as Multifunctional Nanoplatforms

Aqueous Peptide–TiO2 Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms

Prevention of biofilm formation on titanium surfaces modified with conjugated molecules comprised of antimicrobial and titanium-binding peptides

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Aqueous Peptide–TiO₂ Interfaces: Isoenergetic Binding via Either Entropically or Enthalpically Driven Mechanisms