suring the TG2-FN interaction that was applied to HTS of 10,000 Ciloprost customer reviews chemical compounds. The assay has a Z9-factor of 0.7 and identified in robot-assisted screening 90 primary hits; of which 14 were consequently validated. It is anticipated that more SMIs and/or SMIs with improved inhibitory activity will be discovered by using this assay in a larger collection of compounds. Importantly, several of the selected hits demonstrated biological activity in subsequent bio-assays, suggesting that inhibition of the TG2-FN complex formation by the discovered SMIs had measurable functional consequences. The top hits belonged to two structurally unrelated classes of compounds that phenocopied each other, suggesting that the compounds may be specific for the TG2-FN interface. We recognize potential limitations of assays relying on purified labeled proteins that might differ from their native conformations. The specific binding of selected SMIs to the TG2-FN pocket remains to be demonstrated in future analyses. One of the newly discovered SMIs, TG53, was subsequently characterized through complementary assays including doseresponse analyses, ELISA measuring the TG2-FN interaction, and other bioassays quantifying cell adhesion, migration, and proliferation. The focus on TG53 was based on its predicted druglike properties and highest observed inhibitory activity in cell- based assays compared to the other compounds. TG53 performed optimal among selected hits in an ELISA measuring the TG2-FN interaction. Comparison to the effects of an inactive, but structurally similar compound suggests specificity to the TG2-FN complex. However, we cannot exclude off 1357470-29-1 target effects, particularly since the agent displays modest cytotoxic effects at high concentrations. The drug-like potential of TG53 is supported by its predicted physico-chemical properties computed based on its chemical structure by using the ADMET Predictor and ChemSpider software. It is encouraging that TG53 is predicted to be orall