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Plasmonics

, Volume 13, Issue 6, pp 2117–2124 | Cite as

Protein-Metal Interactions Probed by SERS: Lysozyme on Nanostructured Gold Surface

  • N. R. Agarwal
  • M. Tommasini
  • E. Ciusani
  • A. Lucotti
  • S. Trusso
  • P. M. Ossi
Article
  • 114 Downloads

Abstract

Surface-enhanced Raman scattering is a well-established technique for molecular detection at low concentration, which is becoming increasingly popular in the field of biotechnology and health sciences. Since the process is understood in depth, the technique is becoming reliable. In this contribution, we consider another aspect of SERS besides molecular detection, focusing on the binding mechanisms of a complex system such as a protein to the noble metal substrates required by the technique itself. We also show that using a solid nanostructured substrate produced by controlled pulsed laser deposition SERS enables label-free detection of a protein. This is checked on lysozyme as a well-known prototype. Use of solid substrates with controlled morphology proves advantageous over colloidal systems for SERS applications. Moreover, such substrates are superior in terms of shelf life, packaging and ease of shipment.

Keywords

Surface-enhanced Raman scattering Label-free detection Laser ablation Nanostructured substrates Lysozyme Protein binding 

Notes

Funding Information

M.T. acknowledges financial support from PRIN project “Plasmon-enhanced vibrational circular dichroism”. S.T. acknowledges funding by Italian Ministry of Education, University and Research (MIUR) by means of the national Program PON R & C 2007–2013, project “Hippocrates—Sviluppo di Micro e Nano-Tecnologie e Sistemi Avanzati per la Salute dell’uomo (PON0200355)”. Financial support by Polisocial Award 2014 “Controllare l’epilessia nei Paesi in via di sviluppo” (Controlling epilepsy in Developing Countries) is acknowledged by P.M.O.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • N. R. Agarwal
    • 1
    • 2
  • M. Tommasini
    • 1
  • E. Ciusani
    • 3
  • A. Lucotti
    • 1
  • S. Trusso
    • 4
  • P. M. Ossi
    • 5
  1. 1.Dipartimento di Chimica, Materiali e Ingegneria Chimica “Giulio Natta”Politecnico di MilanoMilanItaly
  2. 2.Biointerfaces Institute and Department of Chemistry and Chemical BiologyMcMaster UniversityHamiltonCanada
  3. 3.Istituto Nazionale Neurologico “Carlo Besta”MilanItaly
  4. 4.CNR-IPCF, Istituto per i Processi Chimico-Fisici del CNRMessinaItaly
  5. 5.Dipartimento di Energia & Centre for NanoEngineered MAterials and Surfaces—NEMASPolitecnico di MilanoMilanItaly

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