Key result
A pH/ionic-strength sensor based on the small α-helical protein BBL exhibited a linear response over 4 orders of magnitude in analyte concentration and microsecond response times.
Downhill folding protein modules can be used to create high-performance conformational rheostat sensors with expanded dynamic range and microsecond response times.
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No immediate clinical role; leaves open expanded protein-based sensor research for future cardiovascular applications.
Conformational switches are macromolecules that toggle between two states (active/inactive or folded/unfolded) upon specific binding to a target molecule. These molecular devices provide an excellent scaffold for developing real-time biosensors. Here we take this concept one step beyond to build high-performance conformational rheostat sensors. The rationale is to develop sensors with expanded dynamic range and faster response time by coupling a given signal to the continuous (rather than binary) unfolding process of one-state downhill folding protein modules. As proof of concept we investigate the pH and ionic-strength sensing capabilities of the small α-helical protein BBL. Our results reveal that such a pH/ionic-strength sensor exhibits a linear response over 4 orders of magnitude in analyte concentration, compared to the 2 orders of magnitude for switches, and nearly concentration-independent microsecond response times.
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Cerminara et al. (2012) studied this question. One-state downhill folding protein modules (small α-helical protein BBL) vs. Conformational switches was evaluated on pH and ionic-strength sensing capabilities (dynamic range and response time). A pH/ionic-strength sensor based on the small α-helical protein BBL exhibited a linear response over 4 orders of magnitude in analyte concentration and microsecond response times.
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