Can molecular complementation act as a protein inhibitor?

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yangxu
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I've always wondered about this. Bimolecular fluorescence complementation allows the incorporation of fragments of the green fluorescent protein (GFP) at the N and C-terminus of separate monomers. If the monomers dimerize, the process allows the GFP fragments to come together and form a functional unit that fluoresces, thereby confirming the existence of specific dimers.

Is it possible to use the same method to introduce perhaps peptides or fragments of a small protein into separate monomers, whereby the dimerization process allows the formation of a functional unit recognizable by proteases or antibodies to inhibit the activity of the dimer?
 
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yangxu said:
I've always wondered about this. Bimolecular fluorescence complementation allows the incorporation of fragments of the green fluorescent protein (GFP) at the N and C-terminus of separate monomers. If the monomers dimerize, the process allows the GFP fragments to come together and form a functional unit that fluoresces, thereby confirming the existence of specific dimers.

Is it possible to use the same method to introduce perhaps peptides or fragments of a small protein into separate monomers, whereby the dimerization process allows the formation of a functional unit recognizable by proteases or antibodies to inhibit the activity of the dimer?

A very interesting and well articulated question. I have no answer and am as curious as you are. :)
 
Would it not be easier to simply add a simple tag that can be used to cleave the dimer, once formed?