Your browser doesn't support javascript.
loading
Characterization and molecular docking of tetrapeptides with cellular antioxidant and ACE inhibitory properties from cricket (Acheta domesticus) protein hydrolysate.
Summart, Ratasark; Imsoonthornruksa, Sumeth; Yongsawatdigul, Jirawat; Ketudat-Cairns, Mariena; Udomsil, Natteewan.
Afiliación
  • Summart R; Division of Food Technology, Mahidol University Kanchanaburi Campus, Kanchanaburi, 71150, Thailand.
  • Imsoonthornruksa S; Center for Biomolecular Structure Function and Application, School of Biotechnology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
  • Yongsawatdigul J; School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
  • Ketudat-Cairns M; Center for Biomolecular Structure Function and Application, School of Biotechnology, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand.
  • Udomsil N; Division of Food Technology, Mahidol University Kanchanaburi Campus, Kanchanaburi, 71150, Thailand.
Heliyon ; 10(15): e35156, 2024 Aug 15.
Article en En | MEDLINE | ID: mdl-39166016
ABSTRACT
Wide-ranging bioactivities of enzymatically digested insect protein to produce peptides have been targeted for functional food development. In this study, fractionated peptides obtained from cricket (Acheta domesticus) protein hydrolysate by alcalase digestion were identified and evaluated for their bioactivities. Peptide fractions F44, F45, and F46, isolated through size exclusion chromatography, demonstrated strong cytoprotective effects on SH-SY5Y and HepG2 cells exposed to H2O2. This was evidenced by a 2-fold decrease in reactive oxygen species (ROS) accumulation in the cells and a 3-fold upregulation of genes encoding antioxidant enzymes. The F45 peptide fractions also showed chemical antioxidant activities ranging from approximately 290 to 393 mg trolox/g peptide, measured by DPPH, ABTS, and FRAP assays. Furthermore, F45 demonstrated the highest angiotensin-converting enzyme I (ACE) inhibitory activity, 57.93 %. F45 induced higher levels of Nrf2, SOD1, SOD2, CAT, GSR, and GPx4 gene expression in SH-SY5Y and HepG2 cells compared to cells treated with H2O2 and no peptides (p < 0.05). Cells treated with H2O2 and F45 exhibited significantly increased antioxidant enzyme activity, including SOD, CAT, GSR, and GPx (p < 0.05). The F45B fraction from F45 was sequenced to obtain FVEG and FYDQ tetrapeptides. Molecular docking analysis revealed their high binding affinity to cellular antioxidant enzymes (SOD, CAT, GSR, GPx1, and GPx4), an antioxidant-related protein (Keap1), and ACE. These results suggest that the novel tetrapeptides from Acheta domesticus demonstrate important biological activities, establishing them as significant cellular antioxidant activities and a potential source of antihypertensive peptides.
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Heliyon Año: 2024 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: Heliyon Año: 2024 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Reino Unido