Our proprietary drug discovery platform identifies and develops small molecule allosteric modulators using unique methods. With this technology, we can target disease-related proteins and take full advantage of nature’s sophisticated regulating networks in drug development.
Novel Allosteric Modulators of a7 nACh Receptor
Janssen wanted to identify novel allosteric modulators of the a7 nicotinic acetylcholine receptor, with the ultimate aim to develop novel CNS therapeutics for patients in need.
Beactica's platform enabled the identification of multiple physiologically active novel small molecule modulators acting on previously unexplored allosteric binding sites of the receptor.
Novel Allosteric Hits for USP7
Almac Discovery wanted to identify novel and selective inhibitors for a number of ubiquitin-specific proteases – including USP7 – with the ultimate aim to develop novel cancer therapeutics for patients in need.
Beactica's platform enabled the generation of ”perhaps the most potent small-molecule inhibitor of USP7 to date” which also had extremely high selectivity against other USPs and target classes.
Novel Scaffold for Allosteric Inhibition of HIV-RT
Beactica wanted to identify novel inhibitors of wild type and drug-resistant variants of HIV-1 RT, with the ultimate aim to develop novel HIV therapeutics for patients in need.
Beactica's platform enabled the identification allosteric scaffolds with defined modes of action and desired resistance profiles against key mutant forms of HIV-1 RT.
Insulin Interacting with its Full-Length Receptor
Sanofi wanted to measure the interaction kinetics between insulin and its two binding sites on the full-length insulin receptor, with the ultimate aim to optimize the clinical efficacy of novel insulin analogues.
Results from the collaboration contributed towards the regulatory approval of Insulin lispro Sanofi®, a rapid-acting insulin biosimilar introduced on the market by Sanofi.
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Mechanistic investigation of Afatinib
Boehringer Ingelheim wanted an in-depth understanding of the interaction mechanism of Afatinib (inhibitor of EGFR, HER2, and ErbB4).
The results were a mechanistic rationale for the distinct pharmacological features of Afatinib and thereby an explanation of the clinical activity seen in some patients resistant to antibody or kinase inhibitor therapy.
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