Interfacing porous silicon with biomolecules

Martin J. Sweetman, Sean D. Graney, Nicolas H. Voelcker

Research output: Chapter in Book/Report/Conference proceedingConference PaperOtherpeer-review

4 Citations (Scopus)


The control of protein binding into nanostructured porous surfaces is highly relevant to the development of advanced biosensors and other biodevices. Here, an investigation of the covalent immobilisation of a model protein (albumin) onto porous silicon (pSi) films was conducted using a new alkene linker, the synthesis of which was developed. This alkene linker contained both hydrophobic and hydrophilic (oligoethylene glycol) sections and terminated in a protected thiol. The alkene was attached to freshly etched porous silicon via thermal hydrosilylation, where further surface reactions resulted in the attachment of a maleimido N-hydroxysuccinimidyl (NHS) heterobifunctional crosslinker. Albumin was then covalently immobilised on the porous silicon layer through reaction of the protein's amine groups and the NHS functional group of the crosslinker. Surface modification reactions were monitored by infrared spectroscopy and interferometric reflectance spectroscopy. Protein binding was monitored by infrared spectroscopy, fluorescence imaging and atomic force microscopy.

Original languageEnglish
Title of host publicationBioMEMS and Nanotechnology III
Publication statusPublished - 16 May 2008
Externally publishedYes
EventBioMEMS and Nanotechnology III 2007 - Canberra, Australia
Duration: 5 Dec 20077 Dec 2007

Publication series

NameProgress in Biomedical Optics and Imaging - Proceedings of SPIE
ISSN (Print)1605-7422


ConferenceBioMEMS and Nanotechnology III 2007


  • Biointerfaces
  • Biosensors
  • Hydrosilylation
  • Oligoethylene glycol
  • Porous silicon
  • Protein immobilisation

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