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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la4000846
|2 doi
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| 041 |
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|a eng
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| 100 |
1 |
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|a Coyle, Brandon L
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Carbon-binding designer proteins that discriminate between sp2- and sp3-hybridized carbon surfaces
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|c 2013
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| 336 |
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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| 500 |
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|a Date Completed 26.09.2013
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|a Date Revised 21.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Robust and simple strategies to directly functionalize graphene- and diamond-based nanostructures with proteins are of considerable interest for biologically-driven manufacturing, biosensing, and bioimaging. Here, we identify a new set of carbon-binding peptides that vary in overall hydrophobicity and charge and engineer two of these sequences (Car9 and Car15) within the framework of E. coli thioredoxin 1 (TrxA). We develop purification schemes to recover the resulting TrxA derivatives in a soluble form and conduct a detailed analysis of the mechanisms that underpin the interaction of the fusion proteins with carbonaceous surfaces. Although equilibrium quartz crystal microbalance measurements show that TrxA::Car9 and TrxA::Car15 have similar affinities for sp(2)-hybridized graphitic carbon (Kd = 50 and 90 nM, respectively), only the latter protein is capable of dispersing carbon nanotubes. Further investigation by surface plasmon resonance and atomic force microscopy reveals that TrxA::Car15 interacts with sp(2)-bonded carbon through a combination of hydrophobic and π-π interactions but that TrxA::Car9 exhibits a cooperative mode of binding that relies on a combination of electrostatics and weaker π stacking. Consequently, we find that TrxA::Car9 binds equally well to sp(2)- and sp(3)-bonded (diamondlike) carbon particles whereas TrxA::Car15 is capable of discriminating between the two carbon allotropes. Our results emphasize the importance of understanding both bulk and molecular recognition events when exploiting the adhesive properties of solid-binding peptides and proteins in technological applications
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|a Journal Article
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|a Research Support, N.I.H., Extramural
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Peptides
|2 NLM
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|a Thioredoxins
|2 NLM
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|a 52500-60-4
|2 NLM
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|a Carbon
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|a 7440-44-0
|2 NLM
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| 700 |
1 |
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|a Rolandi, Marco
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Baneyx, François
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 15 vom: 16. Apr., Seite 4839-46
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|g volume:29
|g year:2013
|g number:15
|g day:16
|g month:04
|g pages:4839-46
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|u http://dx.doi.org/10.1021/la4000846
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