Internally quenched fluorogenic substrates with unnatural amino acids for cathepsin G investigation.
Biochimie
; 166: 103-111, 2019 Nov.
Article
em En
| MEDLINE
| ID: mdl-31103725
ABSTRACT
Cathepsin G is one of four members of the neutrophil serine protease family and constitutes an important biological target in various human inflammatory diseases, such as chronic obstructive pulmonary disease, acute respiratory distress syndrome and cystic fibrosis. Many studies have been focused on determining its biological roles, the latest ones concerning its involvement in acute myeloid leukemia, and as such, multiple chemical and biochemical tools were developed to investigate cathepsin G. Nevertheless, most of them lack selectivity or sensitivity and therefore cannot be used in complex systems. Here we present the development of an optimal cathepsin G Internally Quenched Fluorescence (IQF) substrate that incorporates unnatural amino acids causing the increase of its selectivity toward neutrophil elastase and potency in in vitro studies.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Elastase de Leucócito
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Catepsina G
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Corantes Fluorescentes
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article