Publications by authors named "Andrew Campitelli"

Time-resolved adsorption behavior of a human immunoglobin G (hIgG) protein on a hydrophobized gold surface is investigated using multitechniques: quartz crystal microbalance/dissipation (QCM-D) technique; combined surface plasmon resonance (SPR) and Love mode surface acoustic wave (SAW) technique; combined QCM-D and atomic force microscopy (AFM) technique. The adsorbed hIgG forms interfacial structures varying in organization from a submonolayer to a multilayer. An "end-on" IgG orientation in the monolayer film, associated with the surface coverage results, does not corroborate with the effective protein thickness determined from SPR/SAW measurements.

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Prostate-specific antigen (PSA) is a valuable biomarker for prostate cancer screening. We developed a PSA immunoassay on a commercially available surface plasmon resonance biosensor. Our PSA receptor molecule consists of a single domain antigen-binding fragment, cAbPSA-N7, derived from dromedary heavy-chain antibodies and identified after phage display.

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Immunosensors show great potential for the direct detection of biological molecules. The sensitivity of these affinity-based biosensors is dictated by the amount of receptor molecules immobilized on the sensor surface. An enlargement of the sensor area would allow for an increase of the binding capacity, hence a larger amount of immobilized receptor molecules.

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The absorption spectrum of noble metal spherical nanoparticles is known to be strongly influenced by the dielectric constant of the surrounding material, and as such, these particles are well suited for biosensing applications. To perform biosensing using nanoparticles on a substrate, the metal particles are covalently attached onto quartz using an organic adhesion layer of mercaptosilanes. The particles in solution are characterized by UV-vis spectroscopy and transmission electron microscopy, while those attached to the quartz are characterized with UV-vis spectroscopy and atomic force microscopy.

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In a number of applications, e.g. DNA/protein micro-array technology, enzyme-linked immunosorbent assay (ELISA) technology or surface plasmon resonance (SPR) technology, the covalent coupling of proteins to surfaces is required.

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This paper describes a diamond cubic phase with large water channels and determines the temperature dependence of the bilayer thickness in the cubic monoolein/octylglucoside/water system based on time-resolved synchrotron X-ray diffraction data. The X-ray diffraction study established a diamond-type lipid cubic phase with large water channels (Dlarge), which has not been previously reported. It is a distinct phase, different from the diamond cubic phase with normal water channels (Dnormal).

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