Morris Patrick J, Duveau Damien Y, Ceribelli Michele, Tosto Frances Anne, Love Dara N, Scherer Bridget S, Tao Dingyin, Fang Yuhong, Evsen Lale, Kotler Samuel A, LeClair Christopher A, Rai Ganesha, Thomas Craig J, Hoyt Scott B
Division of Preclinical Innovation, National Center for Advancing Translational Sciences, National Institutes of Health, Rockville, Maryland 20850, United States.
J Med Chem. 2025 Aug 28;68(16):17499-17515. doi: 10.1021/acs.jmedchem.5c01027. Epub 2025 Aug 6.
The Large Tumor Suppressor Kinases 1 and 2 (LATS1/2) are serine/threonine kinases that play an essential role in Hippo pathway activation and influence multiple physiological events ranging from organ growth to tissue regeneration. As a result, pharmacological inhibition of LATS1/2 represents a promising strategy for therapeutic intervention in multiple indications. Within, we present the discovery of potent and selective inhibitors of the kinases LATS1 and LATS2. Using a scaffold hopping strategy from the reported AKT inhibitor AT-7867 (1) we pursued a series of structure activity relationship (SAR) studies that dramatically improved potency versus LATS1 and LATS2, while concurrently improving kinome-wide selectivity. ADME properties were further optimized via introduction of conformational restriction into the target molecule, to lead to compound 27 which possesses potent inhibitory activity against both LATS1 and LATS2 and proof of concept activity in wound healing models.
大肿瘤抑制激酶1和2(LATS1/2)是丝氨酸/苏氨酸激酶,在河马通路激活中起关键作用,并影响从器官生长到组织再生等多种生理过程。因此,对LATS1/2进行药理抑制是多种适应症治疗干预的一种有前景的策略。在此,我们展示了LATS1和LATS2激酶强效和选择性抑制剂的发现。利用已报道的AKT抑制剂AT-7867(1)的骨架跳跃策略,我们进行了一系列构效关系(SAR)研究,显著提高了对LATS1和LATS2的效力,同时提高了对整个激酶组的选择性。通过在目标分子中引入构象限制进一步优化了ADME性质,得到了化合物27,其对LATS1和LATS2均具有强效抑制活性,并在伤口愈合模型中具有概念验证活性。