Theoretical Evaluation of Novel Thermolysin Inhibitors from Bacillus thermoproteolyticus. Possible Antibacterial Agents

Simple item page
datacite.alternateIdentifier.citationMOLECULES,Vol.26,,2021
datacite.alternateIdentifier.doi10.3390/molecules26020386
datacite.creatorLamazares, Emilio
datacite.creatorMacLeod Carey, Desmond
datacite.creatorMiranda, Fernando P.
datacite.creatorMena Ulecia, Karel
datacite.date2021
datacite.subject.englishthermolysin
datacite.subject.englishantibacterial agents
datacite.subject.englishdocking
datacite.subject.englishmolecular dynamics
datacite.subject.englishMM-PBSA
datacite.subject.englishADME-Tox
datacite.titleTheoretical Evaluation of Novel Thermolysin Inhibitors from Bacillus thermoproteolyticus. Possible Antibacterial Agents
dc.date.accessioned2021-04-30T17:04:08Z
dc.date.available2021-04-30T17:04:08Z
dc.description.abstractThe search for new antibacterial agents that could decrease bacterial resistance is a subject in continuous development. Gram-negative and Gram-positive bacteria possess a group of metalloproteins belonging to the MEROPS peptidase (M4) family, which is the main virulence factor of these bacteria. In this work, we used the previous results of a computational biochemistry protocol of a series of ligands designed in silico using thermolysin as a model for the search of antihypertensive agents. Here, thermolysin from Bacillus thermoproteolyticus, a metalloprotein of the M4 family, was used to determine the most promising candidate as an antibacterial agent. Our results from docking, molecular dynamics simulation, molecular mechanics Poisson-Boltzmann (MM-PBSA) method, ligand efficiency, and ADME-Tox properties (Absorption, Distribution, Metabolism, Excretion, and Toxicity) indicate that the designed ligands were adequately oriented in the thermolysin active site. The Lig783, Lig2177, and Lig3444 compounds showed the best dynamic behavior; however, from the ADME-Tox calculated properties, Lig783 was selected as the unique antibacterial agent candidate amongst the designed ligands.
dc.identifier.urihttp://repositoriodigital.uct.cl/handle/10925/3813
dc.language.isoen
dc.publisherMDPI
dc.sourceMOLECULES
oaire.resourceTypeArticle
uct.catalogadorWOS
uct.indizacionSCI
Files
Collections
MigraciĆ³n Web of Science