A near-infrared bifc reporter for in vivo imaging of protein-protein interactions

Grigory S. Filonov, Vladislav V. Verkhusha

Research output: Contribution to journalArticlepeer-review

84 Scopus citations


Studies of protein-protein interactions deep in organs and in whole mammals have been hindered by a lack of genetically encoded fluorescent probes in near-infrared region for which mammalian tissues are the most transparent. We have used a near-infrared fluorescent protein iRFP engineered from a bacterial phytochrome as the template to develop an in vivo split fluorescence complementation probe. The domain architecture-based rational design resulted in an iSplit reporter with the spectra optimal for whole-body imaging, high photostability, and high complementation contrast, which compares favorably to that of other available split fluorescent protein-based probes. Successful visualization of interaction of two known protein partners in a living mouse model suggests iSplit as the probe of choice for noninvasive detection of protein-protein interactions in vivo, whereas its fast intracellular degradation enables time-resolved monitoring of repetitive binding events.

Original languageEnglish (US)
Pages (from-to)1078-1086
Number of pages9
JournalChemistry and Biology
Issue number8
StatePublished - Aug 22 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Clinical Biochemistry


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