Protein Engineering and Modeling
Specific alphaReps binding to proteins that do not crystallize when isolated have been selected. The presence of specific alphaRep binders considerably improved the crystallization and was essential to solve the structure of these protein targets.
Due to the presence of disulfide bonds, most antibodies cannot be expressed in a functional form within living cells. AlphaReps are efficiently expressed in living cells, do not aggregate, and can bind their cognate targets . This opens new opportunities for protein interference experiments.
Some alphaReps designed with two domains are folded as a bivalve shell. The closed shell can open when the alphaRep binds its cognate targets. This conformational change can be detected by time resolved fluorescence (FRET) change between a luminescent lanthanide and a quantum dot. This provides the basis of a new type of biosensors.
Protein molecular recognition are not restricted to biological partners. alphaReps binding preferentially to crystallographic plane (111) of Gold surface were selected. These proteins can then be used to change the growth of gold nanoparticles. It also solubilizes the protein coated nanoparticles and offers functional surface on synthetic nanoparticle to drive self-assembly between nano-particles
Artificial metalloenzymes can be engineered by coupling organometallic complexes into an alphaRep protein scaffold. Design and production of enantioselective biohybrids with allosteric properties provides a new class of artificial catalysts for chemical reactions in eco-compatible conditions.