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- W2006535315 abstract "The central tenant of chemical biology and small-molecule drug discovery is that biology can be manipulated using small, organic compounds. Nevertheless, the known drugs act on only ∼1% of the proteome, and the realm of undrugged targets is vast. Protein complexes occupy much of this realm, yet are widely considered “undruggable” or, at best, “challenging.” Thus, there is an opportunity to greatly expand the range of chemical tools and drugs if we can identify which protein-protein interactions are most amenable to small-molecule interference, and what small-molecule discovery approaches are most likely to yield potent and selective modulators. This presentation will describe some of the outstanding issues and promising advances in tackling protein-protein interactions. For example, we note that many protein interfaces are structurally adaptive, and therefore could have low-energy conformations that are amenable to binding small ligands. Additionally, many enzymes are allosterically regulated by protein complexation, and these protein-protein interfaces are also targets for unconventional enzyme inhibitors." @default.
- W2006535315 created "2016-06-24" @default.
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- W2006535315 date "2010-01-01" @default.
- W2006535315 modified "2023-09-30" @default.
- W2006535315 title "Finding Small Molecule Ligands for Protein-Protein Interactions and Other “Undruggable” Targets" @default.
- W2006535315 doi "https://doi.org/10.1016/j.bpj.2009.12.2216" @default.
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