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Functionalized gold nanoparticles as affinity nanoprobes for multiple lectins.

Karuppuchamy Selvaprakash1, Yu-Chie Chen1

  • 1Department of Applied Chemistry, National Chiao Tung University, Hsinchu 300, Taiwan.

Colloids and Surfaces. B, Biointerfaces
|November 18, 2017
PubMed
Summary

This study developed novel gold nanoparticles (Au NPs) from chicken egg white proteins. These Au@cew NPs act as selective affinity probes for detecting specific lectins in complex samples with high sensitivity.

Keywords:
Banana lectinChicken ovalbuminConcanavalin ALectinsRicin

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Area of Science:

  • Nanotechnology
  • Biochemistry
  • Analytical Chemistry

Background:

  • Glycan-lectin interactions are crucial in biological processes.
  • Existing analytical methods for lectin detection often rely on synthetic glycan ligands.
  • Naturally occurring glycoproteins offer an alternative source for glycan-immobilized nanoprobes.

Purpose of the Study:

  • To develop functionalized gold nanoparticles (Au NPs) using readily available chicken egg white (cew) proteins.
  • To create Au@cew NPs decorated with natural glycan ligands for selective lectin detection.
  • To demonstrate the utility of these Au@cew NPs as multiplex affinity probes in conjunction with MALDI-MS.

Main Methods:

  • One-pot synthesis of gold nanoparticles (Au NPs) by reacting cew proteins with tetrachloroaurate.
  • Characterization of Au@cew NPs, confirming encapsulation by ovalbumin and surface decoration with mannose and Galβ(1→4)GlcNAc ligands.
  • Utilizing Au@cew NPs as affinity probes for model lectins (concanavalin A, banana lectin, ricin B).
  • Selective release of bound lectins using specific sugar inhibitors (mannose, glucose, β-lactose).
  • Analysis of released lectins using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS).

Main Results:

  • Generated Au@cew NPs possess hybrid mannose and Galβ(1→4)GlcNAc glycan ligands.
  • Au@cew NPs selectively bind to specific lectins, acting as multiplex affinity probes.
  • Specific sugars effectively released bound lectins from the Au@cew NP-lectin conjugates.
  • MALDI-MS successfully characterized the released lectins.
  • Achieved a low limit of detection (nM range) for model lectins.
  • Demonstrated selective lectin detection from complex samples using the Au@cew NP-based affinity MALDI-MS approach.

Conclusions:

  • Au@cew NPs fabricated from chicken egg white proteins serve as effective natural glycan-based affinity probes.
  • This method enables selective and sensitive detection of multiple lectins.
  • The approach offers a feasible platform for lectin analysis in complex biological samples.