Can molecular complementation act as a protein inhibitor?

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SUMMARY

Bimolecular fluorescence complementation (BiFC) utilizes fragments of the green fluorescent protein (GFP) at the N and C-terminus of separate monomers to confirm dimerization through fluorescence. The discussion explores the potential of using BiFC to introduce peptides or small protein fragments into monomers, enabling the formation of functional units that can be recognized by proteases or antibodies to inhibit dimer activity. The feasibility of this approach raises questions about its practicality compared to simpler methods, such as adding a cleavable tag to the dimer.

PREREQUISITES
  • Understanding of bimolecular fluorescence complementation (BiFC)
  • Knowledge of green fluorescent protein (GFP) structure and function
  • Familiarity with protein dimerization mechanisms
  • Basic concepts of protease and antibody interactions with proteins
NEXT STEPS
  • Research advanced techniques in bimolecular fluorescence complementation (BiFC)
  • Explore methods for peptide tagging and cleavage in protein interactions
  • Investigate the role of proteases in protein dimerization inhibition
  • Study antibody-based approaches for targeting protein complexes
USEFUL FOR

Researchers in molecular biology, biochemists, and anyone interested in protein interaction studies and inhibition techniques.

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?