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.