Abstract This invited Team Profile was created by the Tiwary group, University of Maryland, College Park (USA) and the Seeliger group, Stony Brook University, New York (USA). They recently published an article on the previously made observation through in‐cell screening that the blockbuster cancer drug Gleevec has the same binding affinity, yet different dissociation kinetics against wild‐type and N368S‐mutated Abl kinase. Through all‐atom enhanced molecular dynamics simulations guided by statistical mechanics and information theory, they were able to explain the mechanistic basis of this perplexing observation. Their work has ramifications for how pharmaceutical drugs might experience kinetic resistance due to mutations. “Protein Flexibility and Dissociation Pathway Differentiation Can Explain Onset of Resistance Mutations in Kinases”, M. Shekhar, Z. Smith, M. A. Seeliger, P. Tiwary, Angew. Chem. Int. Ed. 2022, e202200983; Angew. Chem. 2022, e202200983.
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