Peptide-Mediated Formation of Single-Wall Carbon Nanotube Composites

Pender, Mark J.; Sowards, Laura A.; Hartgerink, Jeffrey D.; Stone, Morley O.; Naik, Rajesh R.

doi:10.1021/nl051899r

Cited by 174 publications

(177 citation statements)

References 34 publications

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“…Aptamer-functionalized nanotube electrodes have been shown to detect single bacterial cells in real time 26 . Further, we have recently shown that phage display can be utilized to determine peptide sequences that selectively bind to CNTs and graphene 8,[27][28][29] . This has enabled the generation of bifunctional peptides containing a carbon nanomaterial recognition moiety combined with an analyte binder to non-covalently selfassemble and impart selectivity on graphene sensor arrays.…”

mentioning

confidence: 99%

Graphene-based wireless bacteria detection on tooth enamel

et al. 2012

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Direct interfacing of nanosensors onto biomaterials could impact health quality monitoring and adaptive threat detection. Graphene is capable of highly sensitive analyte detection due to its nanoscale nature. Here we show that graphene can be printed onto water-soluble silk. This in turn permits intimate biotransfer of graphene nanosensors onto biomaterials, including tooth enamel. The result is a fully biointerfaced sensing platform, which can be tuned to detect target analytes. For example, via self-assembly of antimicrobial peptides onto graphene, we show bioselective detection of bacteria at single-cell levels. Incorporation of a resonant coil eliminates the need for onboard power and external connections. Combining these elements yields two-tiered interfacing of peptide-graphene nanosensors with biomaterials. In particular, we demonstrate integration onto a tooth for remote monitoring of respiration and bacteria detection in saliva. overall, this strategy of interfacing graphene nanosensors with biomaterials represents a versatile approach for ubiquitous detection of biochemical targets.

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confidence: 99%

Graphene-based wireless bacteria detection on tooth enamel

et al. 2012

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“…These data presented herein will then be used to help interpret the adsorption behaviour of a known graphene-binding peptide, P1, and its mutant analogue, P1A3. 10,37,68 Simulations of P1 and P1A3 adsorbed at a graphene interface, have been reported previously. 10,37,39,69 However, none of these previous studies used a polarisable FF, or made use of any advanced conformational sampling approaches.…”

Section: Introductionmentioning

confidence: 76%

What makes a good graphene-binding peptide? Adsorption of amino acids and peptides at aqueous graphene interfaces

2015

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Investigation of the non-covalent interaction of biomolecules with aqueous graphene interfaces is a rapidly expanding area. However, reliable exploitation of these interfaces in many applications requires that the links between the sequence and binding of the adsorbed peptide structures be clearly established. Molecular dynamics (MD) simulations can play a key role in elucidating the conformational ensemble of peptides adsorbed at graphene interfaces, helping to elucidate these rules in partnership with experimental characterisation. We apply our recently-developed polarisable force-field for biomolecule-graphene interfaces, GRAPPA, in partnership with advanced simulation approaches, to probe the adsorption behaviour of peptides at aqueous graphene. First we determine the free energy of adsorption of all twenty naturally occurring amino acids (AAs) via metadynamics simulations, providing a benchmark for interpreting peptide-graphene adsorption studies. From these free energies, we find that strong-binding amino acids have flat and/or compact side chain groups, and we relate this behaviour to the interfacial solvent structuring. Second, we apply replica exchange with solute tempering simulations to efficiently and widely sample the conformational ensemble of two experimentally-characterised peptide sequences, P1 and its alanine mutant P1A3, in solution and adsorbed on graphene. For P1 we find a significant minority of the conformational ensemble possesses a helical structure, both in solution and when adsorbed, while P1A3 features mostly extended, random-coil conformations. In solution this helical P1 configuration is stabilised through favourable intra-peptide interactions, while the adsorbed structure is stabilised via interaction of four strongly-binding residues, identified from our metadynamics simulations, with the aqueous graphene interface. Our findings rationalise the performance of the P1 sequence as a known graphene binder.

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“…The library members, detailed in Table 1, range in length from 7-59 amino acids and encode a wide variety of functions such as binding to various inorganic substrates (GBP, CNBP, QBP, MBD and AFP8), nucleation of mineral and metallic nanostructures (A3, CLP12, CT43 and Mms6), and a highly specific catalytic interaction with a protein (SpyTag) 15,[21][22][23][24][25][26][27][28][29][30][31] . Each peptide domain was cloned as C-terminal fusions to CsgA with an intervening six-amino-acid flexible linker (Table 1) and these plasmids were expressed in LSR10 cells to produce 12 different BIND biofilms.…”

Section: Csga Peptide Fusions Retain Amyloid Self-assembly Functionmentioning

confidence: 99%

Programmable biofilm-based materials from engineered curli nanofibres

et al. 2014

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The significant role of biofilms in pathogenicity has spurred research into preventing their formation and promoting their disruption, resulting in overlooked opportunities to develop biofilms as a synthetic biological platform for self-assembling functional materials. Here we present Biofilm-Integrated Nanofiber Display (BIND) as a strategy for the molecular programming of the bacterial extracellular matrix material by genetically appending peptide domains to the amyloid protein CsgA, the dominant proteinaceous component in Escherichia coli biofilms. These engineered CsgA fusion proteins are successfully secreted and extracellularly self-assemble into amyloid nanofibre networks that retain the functions of the displayed peptide domains. We show the use of BIND to confer diverse artificial functions to the biofilm matrix, such as nanoparticle biotemplating, substrate adhesion, covalent immobilization of proteins or a combination thereof. BIND is a versatile nanobiotechnological platform for developing robust materials with programmable functions, demonstrating the potential of utilizing biofilms as large-scale designable biomaterials.

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Peptide-Mediated Formation of Single-Wall Carbon Nanotube Composites

Abstract: The formation of silica- and titania-coated single-wall carbon nanotubes (SWNTs) using a mutlifunctional peptide to both suspend SWNTs and direct the precipitation of silica and titania at room temperature is demonstrated.

Cited by 174 publications

References 34 publications

Graphene-based wireless bacteria detection on tooth enamel

Graphene-based wireless bacteria detection on tooth enamel

What makes a good graphene-binding peptide? Adsorption of amino acids and peptides at aqueous graphene interfaces

Programmable biofilm-based materials from engineered curli nanofibres

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