Streptavidin

The StreptAvidin sensor chips make use of the strong binding between biotin and (strep)avidin.

Hamming, P. H. E. and J. Huskens - Streptavidin Coverage on Biotinylated Surfaces. ACS applied materials & interfaces 13: 58114-58123; (2021). Goto reference

Streptavidin (SAv) monolayers are widely used to immobilize biotinylated proteins, receptors, and DNA. The SAv density on a surface can be varied easily, but the predictability is dependent on the method by which the SAv is immobilized. In this study we show a method to quantitatively predict the SAv coverage on biotinylated surfaces. The method is validated by measuring the SAv coverage on supported lipid bilayers with a range of biotin contents and two different main phase lipids and by using quartz crystal microbalance and localized surface plasmon resonance. We explore a predictive model of the biotin-dependent SAv coverage without any fit parameters. Model and data allow to predict the SAv coverage based on the biotin coverage, in both the low- and high-density regimes. This is of special importance in applications with multivalent binding where control over surface receptor density is required, but a direct measurement is not possible.

Nilsson, P. et al. Real-time monitoring of DNA manipulations using biosensor technology. Analytical Biochemistry 224: 400-408; (1995).

Real time monitoring of DNA manipulations. Using sensor chip SA with streptavidin bound to the surface it is possible to immobilize 5' biotinylated oligonuleotides. With this as a basis, DNA manipulations such as oligo annealing, oligo hybridization, DNA ligation, DNA synthesis and cleavage with endonucleases can be investigated.

Charvolin, D. et al. The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports . Proc.Natl.Acad.Sci.U.S.A 106: 405-410; (2009).

The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports

He, P., S. Faris, R. S. Sagabala, et al. - Cholesterol Chip for the Study of Cholesterol–Protein Interactions Using SPR. Biosensors 12: 788; (2022). Goto reference