{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Richardson LW"],"funding":["Australian Cancer Research Foundation","Wellcome Trust"],"pagination":["e202200306"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9804387"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["17(18)"],"pubmed_abstract":["Plasmepsin X (PMX) is an aspartyl protease that processes proteins essential for Plasmodium parasites to invade and egress from host erythrocytes during the symptomatic asexual stage of malaria. PMX substrates possess a conserved cleavage region denoted by the consensus motif, SFhE (h=hydrophobic amino acid). Peptidomimetics reflecting the P<sub>3</sub> -P<sub>1</sub> positions of the consensus motif were designed and showed potent and selective inhibition of PMX. It was established that PMX prefers Phe in the P<sub>1</sub> position, di-substitution at the β-carbon of the P<sub>2</sub> moiety and a hydrophobic P<sub>3</sub> group which was supported by modelling of the peptidomimetics in complex with PMX. The peptidomimetics were shown to arrest asexual P. falciparum parasites at the schiz"],"journal":["ChemMedChem"],"pubmed_title":["Substrate Peptidomimetic Inhibitors of P. falciparum Plasmepsin X with Potent Antimalarial Activity."],"pmcid":["PMC9804387"],"funding_grant_id":["UNS19392"],"pubmed_authors":["Hodder AN","Jarman KE","Triglia T","Ashton TD","Dans MG","Nguyen N","Favuzza P","Richardson LW","Ngo A","Cowman AF","Sleebs BE"],"additional_accession":[]},"is_claimable":false,"name":"Substrate Peptidomimetic Inhibitors of P. falciparum Plasmepsin X with Potent Antimalarial Activity.","description":"Plasmepsin X (PMX) is an aspartyl protease that processes proteins essential for Plasmodium parasites to invade and egress from host erythrocytes during the symptomatic asexual stage of malaria. PMX substrates possess a conserved cleavage region denoted by the consensus motif, SFhE (h=hydrophobic amino acid). Peptidomimetics reflecting the P<sub>3</sub> -P<sub>1</sub> positions of the consensus motif were designed and showed potent and selective inhibition of PMX. It was established that PMX prefers Phe in the P<sub>1</sub> position, di-substitution at the β-carbon of the P<sub>2</sub> moiety and a hydrophobic P<sub>3</sub> group which was supported by modelling of the peptidomimetics in complex with PMX. The peptidomimetics were shown to arrest asexual P. falciparum parasites at the schiz","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-05-28T06:20:58.781Z","creation":"2025-04-06T09:03:17.821Z"},"accession":"S-EPMC9804387","cross_references":{"pubmed":["35906744"],"doi":["10.1002/cmdc.202200306"]}}