Your browser doesn't support javascript.
loading
Preparation, identification, and inhibitory mechanism of dipeptidyl peptidase IV inhibitory peptides from goat milk whey protein.
Du, Xiaojing; Jiang, Chengyu; Wang, Shan; Jing, Huijuan; Mo, Ling; Ma, Chaoyang; Wang, Hongxin.
Afiliación
  • Du X; The State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China.
  • Jiang C; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, Jiangsu, China.
  • Wang S; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China.
  • Jing H; The State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China.
  • Mo L; Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province, Jiangnan University, Wuxi, Jiangsu, China.
  • Ma C; School of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China.
  • Wang H; The State Key Laboratory of Food Science and Technology, Jiangnan University, Wuxi, Jiangsu, China.
J Food Sci ; 88(8): 3577-3593, 2023 Aug.
Article en En | MEDLINE | ID: mdl-37458288
This study explores potential hypoglycemic mechanisms by preparing and identifying novel dipeptidyl peptidase IV (DPP-IV) inhibitory peptides from goat milk (GM) whey protein. Papain was used to hydrolyze the GM whey protein. After purification by ultrafiltration, the Sephadex column, and preparative RP-HPLC, the peptide inhibited DPP-IV, α-glucosidase, and α-amylase with IC50 of 0.34, 0.37, and 0.72 mg/mL, respectively. To further explore the inhibitory mechanism of peptides on DPP-IV, SPPEFLR, LDADGSY, YPVEPFT, and FNPTY were identified and synthesized for the first time, with IC50 values of 56.22, 52.16, 175.7, and 62.32 µM, respectively. Molecular docking and dynamics results show that SPPEFLR, LDADGSY, and FNPTY bind more tightly to the active pocket of DPP-IV, which was consistent with the in vitro activity. Furthermore, the first three N-terminals of SPPEFLR and FNPTY peptides exhibit proline characteristics and competitively inhibit DPP-IV. Notably, the first N-terminal leucine of LDADGSY may play a key role in inhibiting DPP-IV.
Asunto(s)
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 Asunto principal: Leche / Inhibidores de la Dipeptidil-Peptidasa IV Tipo de estudio: Diagnostic_studies / Prognostic_studies Límite: Animals Idioma: En Revista: J Food Sci Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Leche / Inhibidores de la Dipeptidil-Peptidasa IV Tipo de estudio: Diagnostic_studies / Prognostic_studies Límite: Animals Idioma: En Revista: J Food Sci Año: 2023 Tipo del documento: Article País de afiliación: China Pais de publicación: Estados Unidos