Protein methyltransferases (PMTs) play essential roles in many biological processes. Given the implicated roles of many PMTs on cancer malignancy, many efforts have been made to develop PMT inhibitors. In contrast to genetic perturbation, which depletes full-length proteins, small-molecule inhibitors can act via distinct modes of interaction (MOI) and thus lead to different outcomes even if being designed against the same target. My laboratory leveraged multiple approaches to identify PMT inhibitors with novel MOI. Our sinefungin analogues are SAM-competitive inhibitors with the potency and selectivity for multiple PMTs. The selectivity of these PMT inhibitors largely stems from their abilities to target the distinct conformations. We will present our recent progress in this aspect.<br/>

Exploring novel models of interaction to inhibit protein methyltransferases

253rd National Meeting (2017)

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