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Related Experiment Video

Updated: Jun 13, 2026

Ultrafast Laser-Ablated Nanoparticles and Nanostructures for Surface-Enhanced Raman Scattering-Based Sensing Applications

Ultrafast Laser-Ablated Nanoparticles and Nanostructures for Surface-Enhanced Raman Scattering-Based Sensing Applications

Published on: June 16, 2023

Generic surface modification strategy for sensing applications based on AuSiO2 nanostructures.

Rodolphe Marie¹, Andreas B Dahlin, Jonas O Tegenfeldt

¹Lund University, Division of Solid State Physics, SE-221 00 Lund, Sweden.

|April 23, 2010

Summary

This summary is machine-generated.

This study presents a versatile protocol for creating specific streptavidin patterns on gold and silicon dioxide surfaces. This method enhances protein-adsorption resistance and enables selective binding for various biosensing applications.

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Area of Science:

Biomaterials Science
Surface Chemistry
Nanotechnology

Background:

Developing robust surface modification strategies is crucial for advanced biosensing platforms.
Controlling protein adsorption and localization on different materials remains a challenge.

Purpose of the Study:

To present a generic, material-specific surface modification protocol for creating patterned streptavidin assemblies.
To demonstrate the adaptability of this protocol for both microscale and nanoscale features.

Main Methods:

Utilized thiol-modified poly(ethylene) glycol (thiol-PEG) on gold and poly-L-lysine (PLL) modified PEG (PLL-g-PEG) on SiO(2) for protein-adsorption resistance.
Introduced biotin-modified compounds (thiol-biotin and PLL-g-PEGbiotin) for selective streptavidin binding.
Employed quartz crystal microbalance with dissipation monitoring (QCM-D) for optimization and fluorescence microscopy/localized surface plasmon resonance (LSPR) for verification.

Main Results:

Achieved material-specific protein-adsorption resistance and selective streptavidin binding on patterned gold and SiO(2) surfaces.
Verified the accurate reproduction of microscale patterns and demonstrated compatibility with nanoscale features.
Confirmed that biotinylation did not compromise protein-adsorption resistance.

Conclusions:

The developed protocol offers a generic and adaptable surface modification solution for creating streptavidin patterns.
The strategy is compatible with label-free biosensing techniques like LSPR, making it valuable for diverse biorecognition assays.
The use of commercially available compounds enhances the protocol's practicality for widespread adoption.