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Sensitive and molecular size-selective detection of proteins using a chip-based and heteroliganded gold nanoisland by localized surface plasmon resonance spectroscopy.

Hong S, Lee S, Yi J - Nanoscale Res Lett (2011)

Bottom Line: Their ratios on gold nanoisland were optimized for the sensitive detection of superoxide dismutase (SOD1).This protein has been implicated in the pathology of amyotrophic lateral sclerosis (ALS).Upon exposure of the optimized gold nanoisland to a solution of SOD1 and aggregates thereof, changes in the LSPR spectra were observed which are attributed to the size-selective and covalent chemical binding of SOD1 to the nanoholes.

View Article: PubMed Central - HTML - PubMed

Affiliation: World Class University (WCU) Program of Chemical Convergence for Energy & Environment (C2E2), School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University, Seoul 151-744, Korea. jyi@snu.ac.kr.

ABSTRACT
A highly sensitive and molecular size-selective method for the detection of proteins using heteroliganded gold nanoislands and localized surface plasmon resonance (LSPR) is described. Two different heteroligands with different chain lengths (3-mercaptopionicacid and decanethiol) were used in fabricating nanoholes for the size-dependent separation of a protein in comparison with its aggregate. Their ratios on gold nanoisland were optimized for the sensitive detection of superoxide dismutase (SOD1). This protein has been implicated in the pathology of amyotrophic lateral sclerosis (ALS). Upon exposure of the optimized gold nanoisland to a solution of SOD1 and aggregates thereof, changes in the LSPR spectra were observed which are attributed to the size-selective and covalent chemical binding of SOD1 to the nanoholes. With a lower detection limit of 1.0 ng/ml, the method can be used to selectively detect SOD1 in the presence of aggregates at the molecular level.

No MeSH data available.


Related in: MedlinePlus

Changes in the maximum absorbance peak as a function of the volumetric ratio of a mixed SOD1formulation.
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Figure 4: Changes in the maximum absorbance peak as a function of the volumetric ratio of a mixed SOD1formulation.

Mentions: Upon exposure to the solution of native SOD1 and aggregates thereof, the nanometer-scaled MPA domains (nanoholes) in the mixed SAM can act as a molecular sieve, the SOD1 that are present into the nanoholes then selectively bind to the activated sites on MPA. Figure 4 shows changes in the maximum absorption peak as a function of the volumetric ratio of SOD1 formulations. As the ratio of SOD1 aggregates increases, the change in absorbance peak decreases, and this dependence was dependent on the amount of native SOD1 initially present in the solution. Finally, when the ratio was 1:20, the spectra did not change further. This result suggests that the existance of large amounts of aggregates in the mixture solution may interfere with the an aproach of the native SOD1 to the nanoholes. From the results obtained herein, the heteroliganded gold nanoisland and the detection method permit us to predict the ratio of a protein and macrospecies derived from a protein. Moreover, the method has the portntial for being appplied to other protein fomulations and has considerable potential for use in chip-based diagnoses.


Sensitive and molecular size-selective detection of proteins using a chip-based and heteroliganded gold nanoisland by localized surface plasmon resonance spectroscopy.

Hong S, Lee S, Yi J - Nanoscale Res Lett (2011)

Changes in the maximum absorbance peak as a function of the volumetric ratio of a mixed SOD1formulation.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3211424&req=5

Figure 4: Changes in the maximum absorbance peak as a function of the volumetric ratio of a mixed SOD1formulation.
Mentions: Upon exposure to the solution of native SOD1 and aggregates thereof, the nanometer-scaled MPA domains (nanoholes) in the mixed SAM can act as a molecular sieve, the SOD1 that are present into the nanoholes then selectively bind to the activated sites on MPA. Figure 4 shows changes in the maximum absorption peak as a function of the volumetric ratio of SOD1 formulations. As the ratio of SOD1 aggregates increases, the change in absorbance peak decreases, and this dependence was dependent on the amount of native SOD1 initially present in the solution. Finally, when the ratio was 1:20, the spectra did not change further. This result suggests that the existance of large amounts of aggregates in the mixture solution may interfere with the an aproach of the native SOD1 to the nanoholes. From the results obtained herein, the heteroliganded gold nanoisland and the detection method permit us to predict the ratio of a protein and macrospecies derived from a protein. Moreover, the method has the portntial for being appplied to other protein fomulations and has considerable potential for use in chip-based diagnoses.

Bottom Line: Their ratios on gold nanoisland were optimized for the sensitive detection of superoxide dismutase (SOD1).This protein has been implicated in the pathology of amyotrophic lateral sclerosis (ALS).Upon exposure of the optimized gold nanoisland to a solution of SOD1 and aggregates thereof, changes in the LSPR spectra were observed which are attributed to the size-selective and covalent chemical binding of SOD1 to the nanoholes.

View Article: PubMed Central - HTML - PubMed

Affiliation: World Class University (WCU) Program of Chemical Convergence for Energy & Environment (C2E2), School of Chemical and Biological Engineering, Institute of Chemical Processes, Seoul National University, Seoul 151-744, Korea. jyi@snu.ac.kr.

ABSTRACT
A highly sensitive and molecular size-selective method for the detection of proteins using heteroliganded gold nanoislands and localized surface plasmon resonance (LSPR) is described. Two different heteroligands with different chain lengths (3-mercaptopionicacid and decanethiol) were used in fabricating nanoholes for the size-dependent separation of a protein in comparison with its aggregate. Their ratios on gold nanoisland were optimized for the sensitive detection of superoxide dismutase (SOD1). This protein has been implicated in the pathology of amyotrophic lateral sclerosis (ALS). Upon exposure of the optimized gold nanoisland to a solution of SOD1 and aggregates thereof, changes in the LSPR spectra were observed which are attributed to the size-selective and covalent chemical binding of SOD1 to the nanoholes. With a lower detection limit of 1.0 ng/ml, the method can be used to selectively detect SOD1 in the presence of aggregates at the molecular level.

No MeSH data available.


Related in: MedlinePlus