Protein components for nanodevices

Astier, Yann; Bayley, Hagan; Howorka, Stefan

doi:10.1016/j.cbpa.2005.10.012

Cited by 95 publications

(80 citation statements)

References 53 publications

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“…The work also provides information for designing new binding sites within the lumen of the αHL pore (37) or within other β barrel proteins (21,50) and for using molecular design to devise ways in which to covalently attach CDs within pores (13,51). These areas impact practical applications of nanopore technology including stochastic sensing (8), single-molecule DNA sequencing (9,12,13,52), the use of nanoreactors for the observation of single-molecule chemistry (10), and the construction of nano-and microdevices (11,53), as well as the design of CDs as therapeutic agents (23,24).…”

Section: Resultsmentioning

confidence: 99%

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Banerjee

Mikhailova

Cheley

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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105

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Engineered protein pores have several potential applications in biotechnology: as sensor elements in stochastic detection and ultrarapid DNA sequencing, as nanoreactors to observe singlemolecule chemistry, and in the construction of nano-and microdevices. One important class of pores contains molecular adapters, which provide internal binding sites for small molecules. Mutants of the α-hemolysin (αHL) pore that bind the adapter β-cyclodextrin (βCD) ∼10 4 times more tightly than the wild type have been obtained. We now use single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and highresolution x-ray crystallography to provide definitive structural information on these engineered protein nanopores in unparalleled detail.alpha-hemolysin | single molecule | stochastic sensing | structure | unnatural amino acid M any research groups have used protein engineering to obtain enzymes and antibodies with new properties suited for specific tasks (1-6). Fewer groups have taken on the difficult problem of engineering membrane proteins (7). We have engineered the α-hemolysin protein pore, mindful of several potential applications in biotechnology, including its ability to act as a detector in stochastic sensing (8) and ultrarapid DNA sequencing (9), to serve as a nanoreactor for the observation of singlemolecule chemistry (10) and to act as a component for the construction of nano-and microdevices (11).An important breakthrough in this area, which enabled the stochastic sensing of organic molecules including the detection of DNA bases in the form of nucleoside monophosphates (12, 13), was the discovery of internal molecular adapters, a form of noncovalent protein modification (14). Most useful have been cyclodextrin (CD) adapters, which have until now been used in the absence of detailed structural information about how they work. The present paper is a definitive investigation, which provides such information through the application of a wide variety of technical approaches: single-channel electrical recording, protein engineering including unnatural amino acid mutagenesis, and x-ray crystallography. The studies employing mutagenesis show that the striking interactions seen in the crystal structures also occur in individual pores in lipid bilayers.We reveal that the tight-binding αHL mutants (15) M113N 7 and M113F 7 bind βCD in different orientations within the heptameric pore. In the case of M113N 7 , the top (primary hydroxyls) of the CD ring faces the trans entrance of the pore. In the case of M113F 7 , the bottom (secondary hydroxyls) of the CD ring faces the trans entrance, while the top of the ring is bonded to the pore through remarkable CH-π interactions. Another tight-binding mutant, M113V 7 , can bind the CD in both orientations. These results illustrate the exquisite level of engineering that can be achieved with protein nanopores, which is, for example, far beyond what is possible with solid-state pores. The work also provides information valuable for the design of ...

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Section: Resultsmentioning

confidence: 99%

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Banerjee

Mikhailova

Cheley

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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105

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“…Natural bimolecular assemblies exhibit the selectivity and specificity which can adopt a wide variety of structures that perform an array of functions, and finally they are based on various chemistries (nucleic acids, peptides and proteins, lipids, and carbohydrates) that promote self-assembly in water at neutral pH and ambient temperatures [1]. On the road to these emerging opportunities, proteins represent fertile territory for nanobiotechnology, because they have properties ideal for nano-engineering purposes [2].The building blocks self-assemble and in the presence of ion Ca 2+ salt bridges connect the individual building blocks, resulting in a hollow structure that previously, the kinetics of nanotube formation has been studied as a function of Ca 2+ concentration. The most important functional properties of whey proteins are solubility, viscosity, gel formation, emulsification, foaming, and like many other albumins, the capacity to form nanoparticles (Mehravar et al, 2009) [3] and (H. Hernandez-Sanchez et al, 2012) could obtain nanoparticles of bovine α-lactalbumin α-LA products in the 100 to 200 nm size range so that they could be used as carriers of bioactive compounds [4].…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Esmaeilzadeh¹,

Fakhroueian²,

Esmaeilzadeh³

et al. 2013

ANP

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New water-based nanofluids including unparalleled milk protein α-lactalbumin hollow nano-bio-tubes using low cost, available and advanced partial chemical hydrolysis strategy in bottom-up nano-assembly have been employed in this work. The aqueous sol-gel chemistry in nanotechnology which we selected for this goal offers new fabrication as interesting smart protein nanotubes. The kinds of nanometer sized tubular structures such as waved, helically coiled, bent, bamboo-shaped, bead-like and branched single-walled protein nanotubes (SWPNTs) with a range of 3 -8 nm in outer diameters were produced by this method. Complete characterization for natural produced nanotubes including SEM, TEM images, G bond and D bond in Raman spectroscopy, XRD patterns, DLS (Dynamic Light Scattering) and FTIR analysis were evaluated which they are most significant experiments in synthesized protein nanotubes soluble in clear water nanofluids and stabilization of transparent nanofluids was proved within more than one year after preparation. Various necessary ligand ion salts such as Mn 2+ , Zn 2+ and Ca 2+ or mixtures as bridge makers and producing biological self-assembly hollow SWPNTs were performed and we focused on new chemical technology under specific acidic hydrolysis method not conventional enzymatic proteolysis and applying surfactants, pH reagent, Tris-HCl buffer, polar solvent which could be produced by β-sheet stacked hydrolysed protein α-lactalbumin mechanism under appropriate conditions to achieving high efficiency new protein nanotubes skeleton. They can be promising materials applied in food science, diet nutrition, nanomedicine, nano-biotechnology and surgery.

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“…Using such an approach a wide variety of 'small' and 'simple' biomolecules such as amino acids through to macromolecules such as proteins and DNA and more complex assembled structures thereof have been explored for fabricating novel materials. 1,[14][15][16][17][18][19][20][21][22][23][24][25][26][27] In order to develop this approach further, it is essential to understand in detail how biomolecules interact with inorganic materials, and to be able to identify the 'rules' or 'guiding principles' that govern interaction which could then be used to explain and then predict behaviour. An understanding of biomoleculeinorganic materials interactions would be highly fruitful not only to understand biological mineralization processes but also to design novel materials and processing technologies for applications in fields as diverse as biological imaging and biosensors, implant integration, [28][29][30][31][32] food and drug handling, and electronic materials (Fig.…”

Section: Siddharth V Patwardhanmentioning

confidence: 99%

Interactions of biomolecules with inorganic materials: principles, applications and future prospects

Patwardhan

Perry

2007

J. Mater. Chem.

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The goal of this article is to overview the current understanding of biomolecule-inorganic materials interactions; to identify the 'rules' that govern interaction; to highlight the drawbacks of the present approaches and outline future challenges and opportunities.Please check this proof carefully. Our staff will not read it in detail after you have returned it. Translation errors between word-processor files and typesetting systems can occur so the whole proof needs to be read. Please pay particular attention to: tabulated material; equations; numerical data; figures and graphics; and references. If you have not already indicated the corresponding author(s) please mark their name(s) with an asterisk. Please e-mail a list of corrections or the PDF with electronic notes attached -do not change the text within the PDF file or send a revised manuscript.Please bear in mind that minor layout improvements, e.g. in line breaking, table widths and graphic placement, are routinely applied to the final version.We will publish articles on the web as soon as possible after receiving your corrections; no late corrections will be made.Please return your final corrections, where possible within 48 hours of receipt, by e-mail to: proofs@rsc.org Electronic (PDF) reprints will be provided free of charge to the corresponding author. Enquiries about purchasing paper reprints should be addressed via: http://www.rsc.org/Publishing/ReSourCe/PaperReprints/. Costs for reprints are below: Interactions between inorganic materials and biomolecules at the molecular level, although complex, are commonplace. Examples include biominerals, which are, in most cases, facilitated by and in contact with biomolecules; implantable biomaterials; and food and drug handling. The effectiveness of these functional materials is dependant on the interfacial properties i.e. the extent of molecular level 'association' with biomolecules. The goal of this overview is four-fold: to present biomolecule-inorganic materials interactions and our current understanding using selected examples; to elaborate on approaches that have been used to expose the mechanisms underpinning such interactions; to identify the 'rules' or 'guiding principles' that govern interactions that could be used to explain and hence predict behaviour; and finally to highlight the drawbacks of the present approaches and outline future challenges and opportunities. Reprint costs

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Protein components for nanodevices

Cited by 95 publications

References 53 publications

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Interactions of biomolecules with inorganic materials: principles, applications and future prospects

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Protein components for nanodevices

Cited by 95 publications

References 53 publications

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Molecular bases of cyclodextrin adapter interactions with engineered protein nanopores

Synthesis and Characterization of Various Protein &lt;i&gt;α&lt;/i&gt;-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method

Interactions of biomolecules with inorganic materials: principles, applications and future prospects

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Synthesis and Characterization of Various Protein <i>α</i>-Lactalbumin Nanotubes Structures by Chemical Hydrolysis Method