Self-Assembled Nanochaperones Inhibit the Aggregation of Human Islet Amyloid Polypeptide Associated with Type 2 Diabetes

被引:11
|
作者
Niu, Haihong [1 ]
Hou, Xiaoxue [2 ,3 ]
Zhang, Yanli [1 ]
Wu, Xiaohui [1 ]
Deng, Fei [1 ]
Huang, Fan [2 ,3 ]
Shi, Linqi [1 ]
Ma, Rujiang [1 ]
机构
[1] Nankai Univ, Coll Chem, State Key Lab Med Chem Biol, Key Lab Funct Polymer Mat,Minist Educ, Tianjin 300071, Peoples R China
[2] Chinese Acad Med Sci, Inst Radiat Med, Tianjin Key Lab Radiat Med & Mol Nucl Med, Tianjin 300192, Peoples R China
[3] Peking Union Med Coll, Tianjin 300192, Peoples R China
基金
中国国家自然科学基金;
关键词
QUARTZ-CRYSTAL MICROBALANCE; ARTIFICIAL CHAPERONES; MEMBRANE INTERACTIONS; MOLECULAR CHAPERONES; PYRENE FLUORESCENCE; FIBRIL FORMATION; INSIGHT; MECHANISM; PEPTIDES; DISRUPTION;
D O I
10.1021/acsmacrolett.1c00200
中图分类号
O63 [高分子化学(高聚物)];
学科分类号
070305 ; 080501 ; 081704 ;
摘要
Human islet amyloid polypeptide (hIAPP) aggregation is closely associated with dysfunction and apoptosis of pancreatic beta-cells in type 2 diabetes (T2D). Accordingly, hIAPP amyloid inhibitors have shown promise against T2D. Here, by mimicking the function of natural molecular chaperones, nano-chaperones (nChaps) based on self-assembled polymeric micelles with tunable surface microdomains for T2D treatment are reported. By capturing the aggregation-prone species of hIAPP onto the hydrophobic microdomains and segregating them by hydrophilic PEG chains, this kind of nChaps could effectively prevent hIAPP aggregation, block cell adhesion of hIAPP, facilitate hIAPP aggregates degradation and reduce hIAPP-related cytotoxicity. Therefore, our work will provide useful insights to develop a biomimetic strategy for the treatment of T2D.
引用
收藏
页码:662 / 670
页数:9
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