Cover Feature: Mapping the Pathway and Dynamics of Bestatin Inhibition of the Plasmodium falciparum M1 Aminopeptidase PfA‐M1 (ChemMedChem 23/2018). (4th December 2018)

• Record Type: Journal Article
• Authors: Yang, Wei; Riley, Blake T.; Lei, Xiangyun; Porebski, Benjamin T.; Kass, Itamar; Buckle, Ashley M.; McGowan, Sheena
• Is Part Of: ChemMedChem. Volume 13:Number 23(2018)
• Page Start: 2465
• Page End: 2465
• Publication Date: 2018-12-04
• Subjects: bestatin -- M1 aminopeptidase -- Markov models -- molecular dynamics -- molecular mechanisms; Pharmaceutical chemistry -- Periodicals; 615.19005
• DOI: 10.1002/cmdc.201800741
• Languages: English
• ISSNs: 1860-7179

Abstract

Abstract : 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. onpage 2504 in Issue 23, 2018 (DOI:10.1002/cmdc.201800563 ).