Your browser doesn't support javascript.
loading
Effect of the acyl-group length on the chemoselectivity of the lipase-catalyzed acylation of propranolol-a computational study.
Doerr, Markus; Romero, Alexander; Daza, Martha C.
Afiliação
  • Doerr M; Grupo de Bioquímica Teórica, Universidad Industrial de Santander, Cra. 27 Calle 9, Bucaramanga, Colombia. mhodoerr@uis.edu.co.
  • Romero A; Grupo de Bioquímica Teórica, Universidad Industrial de Santander, Cra. 27 Calle 9, Bucaramanga, Colombia.
  • Daza MC; Grupo de Bioquímica Teórica, Universidad Industrial de Santander, Cra. 27 Calle 9, Bucaramanga, Colombia.
J Mol Model ; 27(7): 198, 2021 Jun 11.
Article em En | MEDLINE | ID: mdl-34115202
The selective N-acylation of 1,2-amino alcohols has been proposed to occur through the proton shuttle mechanism. However, the O-acetylation of propranolol catalyzed by Candida antarctica lipase B is an exception. We investigated the relation between the chemoselectivity of this reaction and the acyl group length. For this purpose, we compared the acyl groups: ethanoyl, butanoyl, octanoyl, and hexadecanoyl. We studied the Michaelis complexes between serine-acylated Candida antarctica lipase B and propranolol, employing a computational approach that involved sampling Michaelis complex conformations through ensemble docking plus consensus scoring and molecular dynamics simulations. The conformations were then classified as near attack conformations for acylation of the amino or hydroxy group. The relative populations of these two classes of conformations were found to be consistent with the experimentally observed chemoselective O-acetylation. We predict that increasing the length of the hydrocarbon chain of the acyl group will cause O-acylation to be unfavorable with respect to N-acylation. The nucleophilic attack of propranolol to the acylated lipase was found to be more favorable through the classical mechanism when compared with the proton shuttle mechanism.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Propranolol / Proteínas Fúngicas / Modelos Moleculares / Lipase Tipo de estudo: Prognostic_studies Idioma: En Revista: J Mol Model Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Propranolol / Proteínas Fúngicas / Modelos Moleculares / Lipase Tipo de estudo: Prognostic_studies Idioma: En Revista: J Mol Model Assunto da revista: BIOLOGIA MOLECULAR Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Colômbia País de publicação: Alemanha