Litcius/Paper detail

Mechanism of covalent binding of ibrutinib to Bruton's tyrosine kinase revealed by QM/MM calculations

Angus Voice, Gary Tresadern, Rebecca M. Twidale, Herman van Vlijmen, Adrian J. Mulholland

2021Chemical Science52 citationsDOIOpen Access PDF

Abstract

) to reach the inactivated BTK/ibrutinib complex. Our results represent the first mechanistic study of BTK inactivation by ibrutinib to consider multiple mechanistic pathways. These findings should aid in the design of covalent drugs that target BTK and other similar targets.

Topics & Concepts

IbrutinibQM/MMBruton's tyrosine kinaseCovalent bondChemistryMechanism (biology)Tyrosine kinaseStereochemistryComputational chemistryBiochemistryMedicineSignal transductionOrganic chemistryPhysicsInternal medicineMolecular dynamicsLeukemiaQuantum mechanicsChronic lymphocytic leukemiaChronic Lymphocytic Leukemia ResearchGalectins and Cancer BiologyMonoclonal and Polyclonal Antibodies Research