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Self-Assembling Enzymatic Nanocomplexes with Polypeptides and Low-Weight Organic Compounds: Preparation, Characterization, and Application of New Antibacterials.
Lyagin, Ilya; Stepanov, Nikolay; Presnov, Denis; Trifonov, Artem; Efremenko, Elena.
Afiliação
  • Lyagin I; Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Stepanov N; Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Presnov D; Skobeltsyn Institute of Nuclear Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Trifonov A; Faculty of Physics, Lomonosov Moscow State University, 119991 Moscow, Russia.
  • Efremenko E; Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia.
Int J Mol Sci ; 24(3)2023 Jan 17.
Article em En | MEDLINE | ID: mdl-36768158
ABSTRACT
The self-assembling of nanosized materials is a promising field for research and development. Multiple approaches are applied to obtain inorganic, organic and composite nanomaterials with different functionality. In the present work, self-assembling nanocomplexes (NCs) were prepared on the basis of enzymes and polypeptides followed by the investigation of the influence of low-molecular weight biologically active compounds on the properties of the NCs. For that, the initially possible formation of catalytically active self-assembling NCs of four hydrolytic enzymes with nine effectors was screened via molecular modeling. It allowed the selection of two enzymes (hexahistidine-tagged organophosphorus hydrolase and penicillin acylase) and two compounds (emodin and naringenin) having biological activity. Further, such NCs based on surface-modified enzymes were characterized by a batch of physical and biochemical methods. At least three NCs containing emodin and enzyme (His6-OPH and/or penicillin acylase) have been shown to significantly improve the antibacterial activity of colistin and, to a lesser extent, polymyxin B towards both Gram-positive bacteria (Bacillus subtilis) and Gram-negative bacteria (Escherichia coli).
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Penicilina Amidase / Emodina Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Penicilina Amidase / Emodina Idioma: En Ano de publicação: 2023 Tipo de documento: Article