Inhibitory effects of epigallocatechin gallate and its glucoside on the human intestinal maltase inhibition

Human intestinal maltase (HMA) is an α-glucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1)...

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Detalles Bibliográficos
Autores principales: Nguyen, Thi Thanh Hanh, Jung, Sun-Hwa, Lee, Sun, Ryu, Hwa-Ja, Kang, Hee-Kyoung, Moon, Young-Hwan, Kim, Young-Min, Kimura, Atsuo, Kim, Doman
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Society for Biotechnology and Bioengineering 2012
Materias:
Research Paper
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7091073/
https://www.ncbi.nlm.nih.gov/pubmed/32218677
http://dx.doi.org/10.1007/s12257-012-0242-8
Descripción
Sumario:Human intestinal maltase (HMA) is an α-glucosidase responsible for the hydrolysis of α-1,4-linkages from the non-reducing end of malto-oligosaccharides. HMA has become an important target in the treatment of type-2 diabetes. In this study, epigallocatechin gallate (EGCG) and EGCG glucoside (EGCG-G1) were identified as inhibitors of HMA by an in vitro assay with IC(50) of 20 ± 1.0 and 31.5 ± 1.0 μM, respectively. A Lineweaver-Burk plot confirmed that EGCG and EGCG-G1 were competitive inhibitors of maltose substrate against HMA and inhibition kinetic constants (K (i)) calculated from a Dixon plot were 5.93 ± 0.26 and 7.88 ± 0.57 μM, respectively. Both EGCG and EGCG-G1 bound to the active site of HMA with numerous hydrophobic and hydrogen bond interactions.

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