In Silico screening of natural small molecules as potential inhibitors of rickettsia protein coded by the IpxC gene
Thomas, Aaron Biju |
Išvados rodo, kad epigalokatechino galatas ir silibinas turi stiprų jungimosi afinitetą su lpxC baltymu, o tai yra daug žadantis potencialas būti švino junginys kuriant naujus antibakterinius agentus, nukreiptus į lipidų A biosintezę Rickettsia conorii. Išsamūs doko tyrimai pabrėžia stiprų epigalokatechino galato ir silibino jungimosi afinitetą su lpxC baltymu UDP-3-O-acil-Nacetilgliukozamino deacetilaze. Šie atradimai rodo, kad abu flavonoidai yra žadantys kaip švino junginiai kuriant naujus antibakterinius agentus, nukreiptus į lipidų A biosintezę Rickettsia conorii. Skirtingi epigallocatechin galato ir silibino sąveikos su fermentu profiliai suteikia vertingų įžvalgų kuriant tikslinius inhibitorius, kurių veiksmingumas ir specifiškumas yra geresnis.
The findings indicate that epigallocatechin gallate and silybin exhibits a strong binding affinity to the lpxC protein, with a promising potential to serve as a lead compound for the development of new antibacterial agents targeting lipid A biosynthesis in Rickettsia conorii. The comprehensive docking studies underscore the strong binding affinity of epigallocatechin gallate and silybin to the lpxC protein UDP-3-O-acyl-N-acetylglucosamine deacetylase. These findings suggest that both flavonoids hold promise as lead compounds for the development of novel antibacterial agents targeting lipid A biosynthesis in Rickettsia conorii. The distinct interaction profiles of epigallocatechin gallate and silybin with the enzyme provide valuable insights for the design of targeted inhibitors with enhanced efficacy and specificity.