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Acido alfa lipoico (ALA) e um dos oxidantes mais poderosos e um cofactor em complexos enzimaticos, apesar de seus mecanismos ainda nao serem conhecidos. A pesquisa por alvos proteicos de ALA e fundamental para compreender seus processos de sinalizacao. Uma abordagem bioinformatica foi usada a fim de se encontrar alvos hipoteticos para ALA usando o servidor Target Fishing Dock (TarFisDock). Contagens de afinidade para os melhores resultados foram calculadas pelo AutoDock Vina. Alvos relevantes incluiram leucotrieno A4 hidrolase, canal de potassio voltagem-dependente, alfa-hidroxiesteroide desidrogenase, epoxido hidrolase, proteinas estas envolvidas no câncer, diabetes, desordens neurologica e cardiovascular. As energias de interacao corrigidas segundo padrao conterpoise foram calculadas para proteinas que ligam R-ALA, e mostraram interacoes R-ALA-residuos favoraveis. A sobreposicao de R-ALA com inibidores conhecidos daquelas proteinas, permitu concluir que R-ALA adota diferentes conformacoes espaciais em seus sitios de ligacao, podendo ser um inibidor fraco plausivel destes alvos e, portanto, este efeito deveria ser considerado quando da realizacao de estudos sobre seus efeitos bioquimicos. Alpha lipoic acid (ALA) is one of the most powerful antioxidants and a cofactor in enzyme complexes, although its mechanisms are still unknown. The search for protein targets of ALA is fundamental to understand its signaling pathways. A bioinformatics approach was used to find hypothetical targets for ALA using the Target Fishing Dock Server (TarFisDock). Affinity scores for the best hits were calculated by AutoDock Vina. Relevant targets included leukotriene A4 hydrolase, voltage gated potassium channel, alpha hydroxysteroid dehydrogenase and epoxide hydrolase, proteins involved in cancer, diabetes, and neurological and cardiovascular disorders. The counterpoise-corrected interaction energies calculated for proteins that bind R-ALA showed favorable interactions R-ALA-residues. Superpositioning of R-ALA with known inhibitors of those proteins, together with the finding that R-ALA adopts different spatial conformations in their binding sites, suggests R-ALA could be a plausible weak inhibitor of these targets, and this effect should be considered when studying its biochemical effects.

Searching of protein targets for alpha lipoic acid