Inhibition of Nonessential Bacterial Targets : Discovery of a Novel Serine O-Acetyltransferase Inhibitor

Show simple item record

dc.contributor.author Pinto de Magalhães, Joana
dc.contributor.author Franko, Nina
dc.contributor.author Raboni, Samanta
dc.contributor.author Annunziato, Giannamaria
dc.contributor.author Tammela, Päivi
dc.contributor.author Bruno, Agostino
dc.contributor.author Bettati, Stefano
dc.contributor.author Mozzarelli, Andrea
dc.contributor.author Pieroni, Marco
dc.contributor.author Cambanini, Barbara
dc.contributor.author Costantino, Gabriele
dc.date.accessioned 2021-02-12T22:51:37Z
dc.date.available 2021-12-18T03:45:28Z
dc.date.issued 2020-05-14
dc.identifier.citation Pinto de Magalhães , J , Franko , N , Raboni , S , Annunziato , G , Tammela , P , Bruno , A , Bettati , S , Mozzarelli , A , Pieroni , M , Cambanini , B & Costantino , G 2020 , ' Inhibition of Nonessential Bacterial Targets : Discovery of a Novel Serine O -Acetyltransferase Inhibitor ' , ACS Medicinal Chemistry Letters , vol. 11 , no. 5 , pp. 790-797 . https://doi.org/10.1021/acsmedchemlett.9b00627
dc.identifier.other PURE: 132798092
dc.identifier.other PURE UUID: 67b929e8-0a8c-416e-8602-aae6e02d9770
dc.identifier.other WOS: 000535281200028
dc.identifier.other ORCID: /0000-0003-4697-8066/work/78162425
dc.identifier.uri http://hdl.handle.net/10138/326416
dc.description.abstract In Upsilon-proteobacteria and Actinomycetales, cysteine biosynthetic enzymes are indispensable during persistence and become dispensable during growth or acute infection. The biosynthetic machinery required to convert inorganic sulfur into cysteine is absent in mammals; therefore, it is a suitable drug target. We searched for inhibitors of Salmonella serine acetyltransferase (SAT), the enzyme that catalyzes the rate-limiting step of L-cysteine biosynthesis. The virtual screening of three ChemDiv focused libraries containing 91 243 compounds was performed to identify potential SAT inhibitors. Scaffold similarity and the analysis of the overall physicochemical properties allowed the selection of 73 compounds that were purchased and evaluated on the recombinant enzyme. Six compounds displaying an IC50 en
dc.format.extent 8
dc.language.iso eng
dc.relation.ispartof ACS Medicinal Chemistry Letters
dc.rights unspecified
dc.rights.uri info:eu-repo/semantics/openAccess
dc.subject Adjuvant therapies
dc.subject Antimicrobial resistance
dc.subject CARBOXYLIC-ACIDS
dc.subject COMPLEX
dc.subject Cysteine biosynthesis
dc.subject ESCHERICHIA-COLI
dc.subject KINETIC MECHANISM
dc.subject L-CYSTEINE
dc.subject Nonessential targets
dc.subject PURIFICATION
dc.subject Serine acetyltransferase
dc.subject 317 Pharmacy
dc.subject 116 Chemical sciences
dc.subject 11832 Microbiology and virology
dc.title Inhibition of Nonessential Bacterial Targets : Discovery of a Novel Serine O-Acetyltransferase Inhibitor en
dc.type Article
dc.contributor.organization Division of Pharmaceutical Biosciences
dc.contributor.organization Drug Research Program
dc.contributor.organization Bioactivity Screening Group
dc.contributor.organization University Management
dc.description.reviewstatus Peer reviewed
dc.relation.doi https://doi.org/10.1021/acsmedchemlett.9b00627
dc.relation.issn 1948-5875
dc.rights.accesslevel openAccess
dc.type.version acceptedVersion

Files in this item

Total number of downloads: Loading...

Files Size Format View
Magalhaes_et_al ... Med_Chem_Lett_Accepted.pdf 885.5Kb PDF View/Open

This item appears in the following Collection(s)

Show simple item record