G proteins serve as intermediate links in signal transmembrane transmission, transferring signals from the cell membrane to effectors and functioning like "postmen". As a component of heterotrimeric G proteins, Gαi1 protein is an essential molecular switch for GPCR-mediated intracellular signal transduction, which operates by switching between an inactive GDP-bound state and an active GTP-bound state. Dysregulation of this switching mechanism is associated with various diseases, such as different types of cancer, making Gαi1 protein an attractive therapeutic target in drug research. Currently, there are several methods for manipulating Gαi1 protein using fluorescent GTP analogs; however, there is a lack of accurate determination of guanine nucleotide binding activity and the active protein fraction.

Recently, Jena Bioscience has successfully developed two novel probes targeting Gαi1: γ-[(4-Aminobutyl)triazolo]-GTP-5-FAM and γ-[(6-Aminohexyl)triazolo]-GTP-5-FAM. These two probes not only exhibit high hydrolytic stability but also demonstrate excellent binding affinity, representing a significant breakthrough in the field of scientific research.

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