| Literature DB >> 33642842 |
Nicholas J Klus1, Khushboo Kapadia2, Peter McDonald3, Anuradha Roy3, Kevin J Frankowski1, Nancy A Muma2, Jeffrey Aubé1.
Abstract
The aberrant protein-protein interaction between calmodulin and mutant huntingtin protein in Huntington's disease patients has been found to contribute to Huntington's disease progression. A high-throughput screen for small molecules capable of disrupting this interaction revealed a sultam series as potent small-molecule disruptors. Diversification of the sultam scaffold afforded a set of 24 analogs or further evaluation. Several structure-activity trends within the analog set were found, most notably a negligible effect of absolute stereochemistry and a strong beneficial correlation with electron-withdrawing aromatic substituents. The most promising analogs were profiled for off-target effects at relevant kinases and, ultimately, one candidate molecule was evaluated for neuroprotection in a neuronal cell model of Huntington's disease.Entities:
Keywords: High-throughput screening; Huntington’s disease; Neurodegeneration; Structure—activity relationship studies
Year: 2020 PMID: 33642842 PMCID: PMC7906539 DOI: 10.1007/s00044-020-02583-8
Source DB: PubMed Journal: Med Chem Res ISSN: 1054-2523 Impact factor: 1.965