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Screening-based design, synthesis and testing of potential Gα protein inhibitors as chemical probes for GPCR signaling

Subject Area Pharmacy
Term from 2019 to 2023
Project identifier Deutsche Forschungsgemeinschaft (DFG) - Project number 431459858
 
Final Report Year 2024

Final Report Abstract

The Gαβγ (guanine nucleotide-binding) heterotrimeric proteins commonly operate as molecular switches to activate (“turn on”) or inactivate (“turn off”) various intracellular signalling pathways in response to stimulated G protein-coupled receptors (GPCRs). Modulation of these G proteins can be exhorted via chemical tools, such as bioactive peptides, which are competent in inhibiting protein-protein interactions (PPIs) upon interactions with distinct binding sites within the protein. Although GPCRs are important targets for the development of pharmaceutical tools (approx. 30% of FDA-approved drugs), notable studies have introduced the major difficulty in drugging the “undruggable” G proteins. The depsipeptides FR900359 (FR) and YM- 254890 (YM) are the only known specific inhibitors described for the G proteins targeting specific the Gαq subunits, highlighting the acute necessity of developing such compounds for the rest subfamilies. In this project, we initially focused on producing, functionally characterizing, and modulating the guanine-nucleotide exchange ability of the Gαi/s subunits. All proteins (Gαi1, Gαs(short) and Gαs(long)) were recombinantly expressed in a prokaryotic system via in-house established protocols which result to the highest reported protein yields. Two novel non-radioactive and fluorescently labelled guanine nucleotide analogues were discovered as high affinity binders to the Gαi1 protein according to fluorescence anisotropy-based assays. Unravelling the fundamental biochemical differences between the two isoforms of the Gαs protein, precedes the future analysis of further Gα subunits. As a second scope of this funded project, two different combinatorial peptide libraries were screened against Gαi/s proteins. Peptides derived from a one-bead-one compound (OBOC) combinatorial library, such as linear the lead compound GPM-1 (and derivatives) indicated a GEM (guanine exchange modulator)-like activity for the Gαi/s∙GDP (the inactive protein state). A set of bicyclic compounds emanated from a one-bead-two compound (OBTC) peptide library revealed GPM-3 as the first peptide described as a class- and state-specific GAP (GTPaseactivating protein)-like modulator of Gαi1∙GMPPNP, and GPM-2 as a potential GEF (guanine nucleotide exchange factor) modulator of Gαi1∙GDP. In conclusion, the aforementioned hits are suggested to serve as possible prodrugs or precursors of compounds exhibiting improved pharmacological properties.

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