Hoon Cho
University of Kentucky
16 Papers
126 Citations
Hoon Cho is an academic researcher from University of Kentucky. The author has contributed to research in topics: Butyrylcholinesterase & Dehydrogenase. The author has an hindex of 11, co-authored 16 publications. Previous affiliations of Hoon Cho include Chosun University & University of Michigan.
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Papers
Computational redesign of human butyrylcholinesterase for anticocaine medication.
TL;DR: The designed BChE mutant has the highest catalytic efficiency against cocaine of all of the reported B ChE mutants, demonstrating that the unique design approach based on transition-state simulation is promising for rational enzyme redesign and drug discovery.
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Most Efficient Cocaine Hydrolase Designed by Virtual Screening of Transition States
Fang Zheng,Wen-Chao Yang,Mei-Chuan Ko,Junjun Liu,Hoon Cho,Daquan Gao,Min Tong,Hsin Hsiung Tai,James H. Woods,Chang-Guo Zhan +9 more
TL;DR: The novel computational design approach has led to discovery of the most efficient cocaine hydrolase, i.e., a human BChE mutant with an approximately 2000-fold improved catalytic efficiency, promising for therapeutic treatment of cocaine overdose and addiction as an exogenous enzyme in human.
Free Energy Perturbation (FEP) Simulation on the Transition States of Cocaine Hydrolysis Catalyzed by Human Butyrylcholinesterase and Its Mutants
TL;DR: The qualitative agreement between the computational and experimental data suggests that the FEP simulations may provide a promising protocol for rational design of high-activity mutants of an enzyme.
Molecular dynamics simulation of cocaine binding with human butyrylcholinesterase and its mutants.
TL;DR: It has been demonstrated that the MD simulation-based computational protocol used in this study is reliable in prediction of the catalytic activity of BChE mutants for (-)-cocaine hydrolysis.
Computational design of a human butyrylcholinesterase mutant for accelerating cocaine hydrolysis based on the transition-state simulation.
TL;DR: An unconventional computational design is reported leading to discovery of a human BChE mutant with a ~151-fold improved catalytic efficiency, which can be used as an exogenous enzyme in human to prevent (−)-cocaine from reaching CNS.
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