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- Cummings, M
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| Max Cummings, Johnson & Johnson PR&D |
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Max Cummings is a Senior Scientist in the Molecular Design and Informatics group at Johnson & Johnson Pharmaceutical Research and Development where he is engaged in various aspects of structure-based drug discovery and design. In addition to supporting various medicinal chemistry projects, his ongoing research interests include protein-protein interactions and small molecule docking.
Max earned his B.Sc. in Chemistry from the University of Winnipeg (1985), M.Sc. in Chemistry from the University of Manitoba (1988) and Ph.D. in Biochemistry from the University of Alberta (1996). His undergraduate and M.Sc. research was in the area of mechanistic enzymology related to acetylcholinesterase. He worked in medicinal chemistry and enzymology at SynPhar Laboratories, Inc., Edmonton from 1988-1996, and in the Department of Biochemistry at the University of Alberta from 1992-1997. His Ph.D. research focused on biochemical applications of modeling and docking. In 1997 Dr.Cummings joined the computational chemistry group at SmithKlineBeecham, King of Prussia, and in 2000 moved to 3-Dimensional Pharmaceuticals, Exton, which later became part of Johnson & Johnson PRD.
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Small Molecule Inhibitors of Protein-Protein Interactions
Max Cummings, Johnson & Johnson PR&D
Normal cell function is dependent upon many protein-protein interactions. Specific inhibitors of protein-protein interactions can serve as useful tools in the study of biochemical pathways, and may ultimately lead to the development of new drugs. Protein-protein interactions are perceived as a potential source of many new targets for drug action, but at the same time are thought to be particularly challenging targets for drug discovery. They are commonly characterized as a distinct target class with respect to small molecule drug discovery. Structures related to the HDM2-p53 protein-protein interaction will serve as an introduction, followed by a more general discussion of selected structural aspects of protein-protein and protein-small molecule binding interactions.
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