Your browser doesn't support javascript.
loading
Procyanidine resists the fibril formation of human islet amyloid polypeptide.
Xu, Jufei; Zheng, Ting; Huang, Xiangyi; Wang, Yanan; Yin, Guowei; Du, Weihong.
Afiliación
  • Xu J; Department of Chemistry, Renmin University of China, Beijing 100872, China.
  • Zheng T; Department of Chemistry, Renmin University of China, Beijing 100872, China.
  • Huang X; Department of Chemistry, Renmin University of China, Beijing 100872, China.
  • Wang Y; Department of Chemistry, Renmin University of China, Beijing 100872, China.
  • Yin G; The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen 518107, China. Electronic address: yingw3@mail.sysu.edu.cn.
  • Du W; Department of Chemistry, Renmin University of China, Beijing 100872, China. Electronic address: whdu@ruc.edu.cn.
Int J Biol Macromol ; 183: 1067-1078, 2021 Jul 31.
Article en En | MEDLINE | ID: mdl-33965498
Human islet amyloid polypeptide (hIAPP) is widely studied due to its close correlation with the pathogenic mechanism of type II diabetes mellitus (T2DM). Bioflavonoids have been used in the neurodegeneration and diabetes studies. However, the structure-activity relationship remains unclear in many of these compounds. In this work, we performed diverse biophysical and biochemical methods to explore the inhibition of procyanidine on hIAPP and compared with that on amyloid-ß (Aß) protein which is linked to Alzheimer's disease (AD). The procyanidine effectively inhibited the aggregation of hIAPP and Aß through hydrophobic and hydrogen bonding interactions, it dissolved the aged fibrils into nanoscale particles. The compound also ameliorated the cytotoxicity and the membrane leakage by reducing the peptide oligomerization. The procyanidine showed better binding affinity and inhibitory effects on peptide aggregation and upregulated the cell viability to hIAPP than to Aß, which could be a prospective inhibitor against hIAPP. This work also offered a possible strategy for T2DM and AD treatments.
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: Catequina / Biflavonoides / Proantocianidinas / Polipéptido Amiloide de los Islotes Pancreáticos / Amiloide Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2021 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
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: Catequina / Biflavonoides / Proantocianidinas / Polipéptido Amiloide de los Islotes Pancreáticos / Amiloide Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2021 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos