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Rapid Nanoprobe Signal Enhancement by In Situ Gold Nanoparticle Synthesis

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An optical biosensing platform for proteinase activity using gold nanoparticles.

Yao-Chen Chuang¹, Jung-Chun Li, Sz-Hau Chen

¹Department of Biological Science and Technology, National Chiao Tung University, Hsinchu, Taiwan.

|May 18, 2010

Summary

This study developed a gold nanoparticle-based biosensor for detecting proteinase activity. The sensor utilizes changes in surface plasmon resonance, causing a visible color shift from red to blue upon enzyme digestion.

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Area of Science:

Nanotechnology
Biochemistry
Analytical Chemistry

Background:

Surface plasmon resonance (SPR) of gold nanoparticles (AuNPs) is sensitive to aggregation, size, shape, and chemical modification.
Proteinase activity assays are crucial for diagnosing diseases and understanding biological processes.

Purpose of the Study:

To establish an optical biosensing platform for proteinase activity assay using the SPR property of AuNPs.
To develop a colorimetric method for detecting proteinase activity that is observable with the naked eye.

Main Methods:

13-nm AuNPs were modified with gelatin as a substrate and 6-mercaptohexan-1-ol (MCH).
Proteinase digestion (trypsin or gelatinase) caused AuNPs aggregation due to loss of shelter and increased MCH attraction.
AuNPs aggregation was monitored by the red shift of surface plasmon absorption and a color change from red to blue.

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Quantitative analysis was performed using the absorption ratio A(625)/A(525).

Main Results:

A visible color change from red to blue indicated proteinase activity.
A linear correlation was established between the absorption ratio and trypsin activity (1.25 x 10(-1) to 1.25 x 10(2) U).
A linear correlation was established between the absorption ratio and matrix metalloproteinase-2 activity (50 ng/mL to 600 ng/mL).

Conclusions:

The developed AuNPs-based platform is effective for detecting proteinase activity.
The colorimetric shift provides a simple, naked-eye observable method for proteinase detection.
The platform offers quantitative analysis of trypsin and matrix metalloproteinase-2 activity.