Number 1 again
Our method for detection of vasoactive receptor aggregation by FRET was again the number 1 publication in its scientific domain.
In 2011, we established a method, which enables to detect and monitor the interaction between two different membrane receptors in intact cells by fluorescence resonance energy transfer (FRET). FRET is capable to detect protein-protein interactions in close proximity, in the range of 1-10 nm in distance.
The technique ended a decade of discussion about the existence of heterodimerization between the angiotensin II AT1 receptor and the bradykinin B2 receptor. And in December 2014, BioMedLib, once again, recognized the article as number 1 (in its domain).
The established method relies on a cleavable signal peptide, which enhances cell surface delivery of a fluorescent protein-labeled membrane receptor. Results demonstrated a FRET efficiency of 24.7 % between AT1R-Cerulean and B2R-EYFP in intact cells reflecting the close interaction between AT1R and B2R indicative of heterodimerization.
external pageThe technique can be found here.