Sulfur‐based molecules containing biotin and hydroxyl groups have been used to create a wide variety of self‐assembled monolayers on gold surfaces. Surface plasmon resonance has been used to study in situ the binding of streptavidin to these monolayers from solution. The self‐assembled monolayers allow a high degree of control over the surface properties. The choice of an appropriate biotin‐containing molecule, with a spacer segment, and the dilution of this molecule within the monolayer by hydroxythiols, allows optimization of the binding properties of the monolayer—nonspecific interactions between streptavidin and the surface are below detection limits, and specific binding between the streptavidin and biotin groups can be maximized.
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