BioGold SPR Substrates

Surface plasmon resonance (SPR) occurs when light energy couples into the electromagnetic field at a metal-coated surface. The reflectivity of the incident light is inverse to the extent of plasmon resonance, and is determined by the identity and the thickness of the metal layer, the angle of incidence, the wavelength of the incident light, and the refractive index of the medium at the interface. Because the refractive index is proportional to the amount of adsorbate at the surface, SPR has been used as a quantitative, sensitive, and label-free technique for measuring the binding kinetics of proteins, DNA, and small molecules, to surface immobilized capture agents. Using SPR in an imaging mode, high throughput analysis of proteins and DNA has also been demonstrated.

BioGold™ SPR substrates are available on 1mm thick, UltraFlat, premium glass:

• BioGold SPR-25 is available with either titanium or chromium binding layer, coated with 25 +/- 5 nm gold (99.9% pure);this sensor is translucent

• BioGold SPR-35 is available with either titanium or chromium binding layer, coated with 35 +/- 5 nm gold (99.9% pure)
• BioGold SPR-45 is available with either titanium or chromium binding layer, coated with 45 +/- 5 nm gold (99.9% pure)

Applicable notes and publications utilizing gold biosensors:

1. Shumaker-Parry, J.S., et al. Probing Protein:DNA Interactions Using a Uniform Monolayer of DNA and Surface Plasmon Resonance. in Proceedings of SPIE Photonics West Conference,
International Biomedical Optics Symposium. 2000. San Jose, CA: SPIE.
2. Lu, H.B., et al., Protein contact printing for a surface plasmon resonance biosensor with onchip referencing. Sensors and Actuators B-Chemical, 2001. 74(1-3): p. 91-99.
3. Shumaker-Parry, J., R.A. Aebersold, and C.T. Campbell, Parallel, Quantitative Measurement
of Protein Binding to a 120-Element Double-Stranded DNA Array in Real Time Using SPR
Microscopy. Anal. Chem., subm.
4. Jung, L.S., et al., Quantification of tight binding to surface-immobilized phospholipid vesicles using surface plasmon resonance: Binding constant of phospholipase A(2). Journal of the American Chemical Society, 2000. 122(17): p. 4177-4184.
5. Shumaker-Parry, J., et al., Microspotting Streptavidin and Double-Stranded DNA Arrays on
Gold for High-Throughput Studies of Protein - DNA Interactions by SPR Microscopy. Anal.
Chem., subm.
6. Bulyk, M.L., et al., Quantifying DNA-protein interactions by double-stranded DNA arrays.
Nature Biotechnology, 1999. 17: p. 573-7.