Hydrophobicity-driven self-assembly of protein and silver nanoparticles for protein detection using surface-enhanced Raman scattering

Mehmet Kahraman, Ben N. Balz, Sebastian Wachsmann-Hogiu

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Surface-enhanced Raman scattering (SERS) is a promising analytical technique for the detection and characterization of biological molecules and structures. The role of hydrophobic and hydrophilic surfaces in the self-assembly of protein-metallic nanoparticle structures for label-free protein detection is demonstrated. Aggregation is driven by both the hydrophobicity of the surface as well as the charge of the proteins. The best conditions for obtaining a reproducible SERS signal that allows for sensitive, label-free protein detection are provided by the use of hydrophobic surfaces and 16 × 1011 NPs per mL. A detection limit of approximately 0.5 μg mL-1 is achieved regardless of the proteins' charge properties and size. The developed method is simple and can be used for reproducible and sensitive detection and characterization of a wide variety of biological molecules and various structures with different sizes and charge status.

Original languageEnglish (US)
Pages (from-to)2906-2913
Number of pages8
JournalAnalyst
Volume138
Issue number10
DOIs
StatePublished - May 21 2013

Fingerprint

Silver Proteins
Raman Spectrum Analysis
hydrophobicity
Hydrophobicity
Hydrophobic and Hydrophilic Interactions
Nanoparticles
Self assembly
Raman scattering
silver
Silver
scattering
Proteins
protein
Labels
Metal Nanoparticles
Molecules
Limit of Detection
analytical method
Agglomeration
nanoparticle

ASJC Scopus subject areas

  • Analytical Chemistry
  • Spectroscopy
  • Electrochemistry
  • Biochemistry
  • Environmental Chemistry
  • Medicine(all)

Cite this

Hydrophobicity-driven self-assembly of protein and silver nanoparticles for protein detection using surface-enhanced Raman scattering. / Kahraman, Mehmet; Balz, Ben N.; Wachsmann-Hogiu, Sebastian.

In: Analyst, Vol. 138, No. 10, 21.05.2013, p. 2906-2913.

Research output: Contribution to journalArticle

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