Densely substituted piperidines as a new class of elastase inhibitors: Synthesis and molecular modeling studies.
Arch Pharm (Weinheim)
; 352(8): e1900061, 2019 Aug.
Article
em En
| MEDLINE
| ID: mdl-31338866
ABSTRACT
Elastase is the only enzyme that has the capability to degrade elastin and collagen, the two proteins essential for skin and bones. The synthesis of some densely substituted piperidines functionalized with the trifluoromethyl group (4a-j) was carried out. The newly prepared compounds were subjected to elastase enzyme inhibitory potential and antioxidant activity assays. Among the series, 4i (IC50 = 0.341 ± 0.001 µM) exhibited the maximum inhibition against elastase. Binding analysis delineated that the fluorine atom of ligand 4i showed hydrogen and hydrophobic bonds with Thr41 and Thr96, with bond distances of 3.84 and 5.631 Å, respectively. The obtained results indicate that these trifluoromethyl functionalized piperidine derivatives could be considered as potential candidates to treat skin disorders.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Piperidinas
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Elastase Pancreática
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Inibidores de Serina Proteinase
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Hidrocarbonetos Fluorados
Limite:
Animals
Idioma:
En
Revista:
Arch Pharm (Weinheim)
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Paquistão