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Optimizing Nanoplasmonic Biosensor Sensitivity with Orientated Single Domain Antibodies.

Raphael MP, Christodoulides JA, Byers JM, Anderson GP, Liu JL, Turner KB, Goldman ER, Delehanty JB - Plasmonics (2015)

Bottom Line: We demonstrate that orientated single domain antibodies (sdAb) can optimize nanoplasmonic sensitivity by comparing three anti-ricin sdAb constructs to biotin-neutravidin, a model system for small and highly orientated ligand studies.LSPR imaging of electrostatically orientated sdAb exhibited a ricin sensitivity equivalent to that of the biotinylated LSPR biosensors for neutravidin.These results, combined with the facts that sdAb are highly stable and readily produced in bacteria and yeast, build a compelling case for the increased utilization of sdAbs in nanoplasmonic applications.

View Article: PubMed Central - PubMed

Affiliation: Bioelectronics and Sensing, Code 6363, Naval Research Laboratory, 4555 Overlook Ave SW, Washington, DC 20375 USA.

ABSTRACT

Localized surface plasmon resonance (LSPR) spectroscopy and imaging are emerging biosensor technologies which tout label-free biomolecule detection at the nanoscale and ease of integration with standard microscopy setups. The applicability of these techniques can be limited by the restrictions that surface-conjugated ligands must be both sufficiently small and orientated to meet analyte sensitivity requirements. We demonstrate that orientated single domain antibodies (sdAb) can optimize nanoplasmonic sensitivity by comparing three anti-ricin sdAb constructs to biotin-neutravidin, a model system for small and highly orientated ligand studies. LSPR imaging of electrostatically orientated sdAb exhibited a ricin sensitivity equivalent to that of the biotinylated LSPR biosensors for neutravidin. These results, combined with the facts that sdAb are highly stable and readily produced in bacteria and yeast, build a compelling case for the increased utilization of sdAbs in nanoplasmonic applications.

No MeSH data available.


a LSPRi of nine arrays, each array consisting of 400 nanostructures. The image is false colored red to indicate the resonance wavelength of 635 nm. b Scanning electron microscopy of an array of 400 nanostructures. c LSPRi response to 100 nM ricin for C8-zip, C8, and D12f-rhiz surfaces compared to that of a biotinylated surface for 100 nM neutravidin
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Fig4: a LSPRi of nine arrays, each array consisting of 400 nanostructures. The image is false colored red to indicate the resonance wavelength of 635 nm. b Scanning electron microscopy of an array of 400 nanostructures. c LSPRi response to 100 nM ricin for C8-zip, C8, and D12f-rhiz surfaces compared to that of a biotinylated surface for 100 nM neutravidin

Mentions: For the corresponding nanoplasmonic response studies, a functionalization protocol identical to that used for the SPR study in Fig. 2a was applied to the gold nanostructures of the custom-made LSPR chips. Response data to 100 nM ricin were determined by averaging the mean intensity of nine arrays, each array consisting of 400 nanostructures (Fig. 4a, b). As with the SPR results, the C8-zip surface was the most sensitive of the three ligands, with a saturation response that was 104 % greater than that of C8 and 61 % greater than that of D12f-rhiz (Fig. 4c).Fig. 4


Optimizing Nanoplasmonic Biosensor Sensitivity with Orientated Single Domain Antibodies.

Raphael MP, Christodoulides JA, Byers JM, Anderson GP, Liu JL, Turner KB, Goldman ER, Delehanty JB - Plasmonics (2015)

a LSPRi of nine arrays, each array consisting of 400 nanostructures. The image is false colored red to indicate the resonance wavelength of 635 nm. b Scanning electron microscopy of an array of 400 nanostructures. c LSPRi response to 100 nM ricin for C8-zip, C8, and D12f-rhiz surfaces compared to that of a biotinylated surface for 100 nM neutravidin
© Copyright Policy - OpenAccess
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4644190&req=5

Fig4: a LSPRi of nine arrays, each array consisting of 400 nanostructures. The image is false colored red to indicate the resonance wavelength of 635 nm. b Scanning electron microscopy of an array of 400 nanostructures. c LSPRi response to 100 nM ricin for C8-zip, C8, and D12f-rhiz surfaces compared to that of a biotinylated surface for 100 nM neutravidin
Mentions: For the corresponding nanoplasmonic response studies, a functionalization protocol identical to that used for the SPR study in Fig. 2a was applied to the gold nanostructures of the custom-made LSPR chips. Response data to 100 nM ricin were determined by averaging the mean intensity of nine arrays, each array consisting of 400 nanostructures (Fig. 4a, b). As with the SPR results, the C8-zip surface was the most sensitive of the three ligands, with a saturation response that was 104 % greater than that of C8 and 61 % greater than that of D12f-rhiz (Fig. 4c).Fig. 4

Bottom Line: We demonstrate that orientated single domain antibodies (sdAb) can optimize nanoplasmonic sensitivity by comparing three anti-ricin sdAb constructs to biotin-neutravidin, a model system for small and highly orientated ligand studies.LSPR imaging of electrostatically orientated sdAb exhibited a ricin sensitivity equivalent to that of the biotinylated LSPR biosensors for neutravidin.These results, combined with the facts that sdAb are highly stable and readily produced in bacteria and yeast, build a compelling case for the increased utilization of sdAbs in nanoplasmonic applications.

View Article: PubMed Central - PubMed

Affiliation: Bioelectronics and Sensing, Code 6363, Naval Research Laboratory, 4555 Overlook Ave SW, Washington, DC 20375 USA.

ABSTRACT

Localized surface plasmon resonance (LSPR) spectroscopy and imaging are emerging biosensor technologies which tout label-free biomolecule detection at the nanoscale and ease of integration with standard microscopy setups. The applicability of these techniques can be limited by the restrictions that surface-conjugated ligands must be both sufficiently small and orientated to meet analyte sensitivity requirements. We demonstrate that orientated single domain antibodies (sdAb) can optimize nanoplasmonic sensitivity by comparing three anti-ricin sdAb constructs to biotin-neutravidin, a model system for small and highly orientated ligand studies. LSPR imaging of electrostatically orientated sdAb exhibited a ricin sensitivity equivalent to that of the biotinylated LSPR biosensors for neutravidin. These results, combined with the facts that sdAb are highly stable and readily produced in bacteria and yeast, build a compelling case for the increased utilization of sdAbs in nanoplasmonic applications.

No MeSH data available.