Literature DB >> 25341419

Plasmodium falciparum M1-aminopeptidase: a promising target for the development of antimalarials.

Jorge González-Bacerio, Rafael Fando, Alberto del Monte-Martínez, Jean-Louis Charli, María de los Á Chávez1.   

Abstract

Malaria is a devastating human parasitic disease that receives enhanced attention due to the emergence of resistance to traditional drugs. Thus, the search for new molecular targets is a major goal. PfAM1 is an aminopeptidase from Plasmodium falciparum, William H. Welch 1897, belonging to the M1 family of metalloproteases, which is a promising target of inhibitors to block the intra-erythrocytic stages of the parasite. Since its identification in 1998, many efforts have been done to validate PfAM1 as an appropriate target of antimalarials. The present work is a critical review of the main structural, functional and kinetic characteristics of PfAM1, as well as a summary of the effects of key inhibitors at molecular and cellular levels. The systematization of experimental results should contribute to a better understanding of the properties of PfAM1 as a target of antimalarials and promote research projects focused on the development of PfAM1 inhibitors.

Entities:  

Mesh:

Substances:

Year:  2014        PMID: 25341419     DOI: 10.2174/1389450115666141024115641

Source DB:  PubMed          Journal:  Curr Drug Targets        ISSN: 1389-4501            Impact factor:   3.465


  7 in total

1.  IgG antibody response against Plasmodium falciparum aminopeptidase 1 antigen in Gabonese children living in Makokou and Franceville.

Authors:  S L Oyegue-Liabagui; R-K Imboumy-Limoukou; C L Kouna; F Bangueboussa; M Schmitt; I Florent; J B Lekana-Douki
Journal:  Clin Exp Immunol       Date:  2020-02-21       Impact factor: 4.330

2.  Two cap residues in the S1 subsite of a Plasmodium falciparum M1-family aminopeptidase promote broad specificity and enhance catalysis.

Authors:  Matthew Rosati; Seema Dalal; Michael Klemba
Journal:  Mol Biochem Parasitol       Date:  2017-08-12       Impact factor: 1.759

3.  Selective inhibition of PfA-M1, over PfA-M17, by an amino-benzosuberone derivative blocks malaria parasites development in vitro and in vivo.

Authors:  Lotfi Bounaadja; Marjorie Schmitt; Sébastien Albrecht; Elisabeth Mouray; Céline Tarnus; Isabelle Florent
Journal:  Malar J       Date:  2017-09-21       Impact factor: 2.979

4.  P1' Residue-Oriented Virtual Screening for Potent and Selective Phosphinic (Dehydro) Dipeptide Inhibitors of Metallo-Aminopeptidases.

Authors:  Michał Talma; Artur Mucha
Journal:  Biomolecules       Date:  2020-04-24

5.  Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases.

Authors:  Emmanuel Salomon; Marjorie Schmitt; Anil Kumar Marapaka; Athanasios Stamogiannos; Germain Revelant; Céline Schmitt; Sarah Alavi; Isabelle Florent; Anthony Addlagatta; Efstratios Stratikos; Céline Tarnus; Sébastien Albrecht
Journal:  Molecules       Date:  2018-10-11       Impact factor: 4.411

6.  Activity profiling of peptidases in Angiostrongylus costaricensis first-stage larvae and adult worms.

Authors:  Karina M Rebello; James H McKerrow; Ester M Mota; Anthony J O'Donoghue; Ana Gisele C Neves-Ferreira
Journal:  PLoS Negl Trop Dis       Date:  2018-10-31

7.  Steered molecular dynamics simulations reveal critical residues for (un)binding of substrates, inhibitors and a product to the malarial M1 aminopeptidase.

Authors:  Daniel S Moore; Conor Brines; Heather Jewhurst; John P Dalton; Irina G Tikhonova
Journal:  PLoS Comput Biol       Date:  2018-10-31       Impact factor: 4.475

  7 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.