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Can molecular complementation act as a protein inhibitor?

  1. Dec 5, 2008 #1
    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?
     
  2. jcsd
  3. Dec 6, 2008 #2
    A very interesting and well articulated question. I have no answer and am as curious as you are. :)
     
  4. Dec 10, 2008 #3
    Would it not be easier to simply add a simple tag that can be used to cleave the dimer, once formed?
     
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