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Cover Feature: Mapping the Pathway and Dynamics of Bestatin Inhibition of the Plasmodium falciparum M1 Aminopeptidase Pf A‐M1 (ChemMedChem 23/2018)
Author(s) -
Yang Wei,
Riley Blake T.,
Lei Xiangyun,
Porebski Benjamin T.,
Kass Itamar,
Buckle Ashley M.,
McGowan Sheena
Publication year - 2018
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201800741
Subject(s) - aminopeptidase , computational biology , drug discovery , cover (algebra) , chemistry , superfamily , snapshot (computer storage) , molecular dynamics , drug target , plasmodium falciparum , feature (linguistics) , biochemistry , biology , computer science , amino acid , malaria , receptor , computational chemistry , leucine , mechanical engineering , linguistics , philosophy , engineering , immunology , operating system
The Cover Feature shows interactions of the aminopeptidase inhibitor bestatin with the antimalarial drug target Pf A‐M1. The development of inhibitors/drug candidates typically involves understanding the precise molecular details of their interactions with their targets. X‐ray crystallography can reveal the atomic interactions between the two molecules but is a static ‘snapshot’ of the final state and provides no information on the events before, or in indeed after association. Using molecular simulation techniques, we have mapped the route by which bestatin can dissociate from Pf A‐M1. This analysis provides important knowledge that may be exploited in the design of new inhibitors/drugs that target Pf A‐M1 and the large M1 aminopeptidase superfamily. More information can be found in the Full Paper by Sheena McGowan et al. on page 2504 in Issue 23, 2018 (DOI: 10.1002/cmdc.201800563).