Can molecular complementation act as a protein inhibitor?

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Bimolecular fluorescence complementation (BiFC) utilizes fragments of green fluorescent protein (GFP) at the N and C-terminus of separate monomers, allowing them to fluoresce upon dimerization, thus confirming specific interactions. The discussion explores the potential of applying this method to introduce peptides or small protein fragments into monomers, enabling the formation of a functional unit that could be recognized by proteases or antibodies to inhibit dimer activity. While the concept is intriguing, there is uncertainty about its feasibility. One suggestion is to consider using a simple tag for cleavage of the dimer once formed, which may offer a more straightforward approach.
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?
 
https://www.discovermagazine.com/the-deadliest-spider-in-the-world-ends-lives-in-hours-but-its-venom-may-inspire-medical-miracles-48107 https://en.wikipedia.org/wiki/Versutoxin#Mechanism_behind_Neurotoxic_Properties https://www.sciencedirect.com/science/article/abs/pii/S0028390817301557 (subscription or purchase requred) The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel...
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