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The molecular basis of distinct aggregation pathways of islet amyloid polypeptide

หน่วยงาน Nanyang Technological University, Singapore

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ชื่อเรื่อง : The molecular basis of distinct aggregation pathways of islet amyloid polypeptide
นักวิจัย : Wei, Lei , Jiang, Ping , Xu, Weixin , Li, Hai , Zhang, Hua , Yan, Liang Yu , Chan-Park, Mary B. , Liu, Xue-Wei , Tang, Kai , Mu, Yuguang , Pervushin, Konstantin
คำค้น : DRNTU::Science::Biological sciences::Biochemistry.
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2554
อ้างอิง : Wei, L., Jiang, P., Xu, W., Li, H., Zhang, H., Yan, L., Chan-Park, M. B., Liu, X.-W., Tang, K., Mu, Y., & Pervushin, K. (2011). The Molecular Basis of Distinct Aggregation Pathways of Islet Amyloid Polypeptide. Journal of Biological Chemistry, 286(8), 6291-6300. , 0021-9258 , http://hdl.handle.net/10220/8323 , http://dx.doi.org/10.1074/jbc.M110.166678
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Journal of Biological Chemistry
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

Abnormal aggregation of islet amyloid polypeptide (IAPP) into amyloid fibrils is a hallmark of type 2 diabetes. In this study, we investigated the initial oligomerization and subsequent addition of monomers to growing aggregates of human IAPP at the residue-specific level using NMR, atomic force microscopy, mass spectroscopy, and computational simulations. We found that in solution IAPPs rapidly associate into transient low-order oligomers such as dimers and trimers via interactions between histidine 18 and tyrosine 37. This initial event is proceeded by slow aggregation into higher-order spherical oligomers and elongated fibrils. In these two morphologically distinct types of aggregates IAPPs adopt structures with markedly different residual flexibility. Here we show that the anti-amyloidogenic compound resveratrol inhibits oligomerization and amyloid formation via binding to histidine 18, supporting the finding that this residue is crucial for on-pathway oligomer formation.

บรรณานุกรม :
Wei, Lei , Jiang, Ping , Xu, Weixin , Li, Hai , Zhang, Hua , Yan, Liang Yu , Chan-Park, Mary B. , Liu, Xue-Wei , Tang, Kai , Mu, Yuguang , Pervushin, Konstantin . (2554). The molecular basis of distinct aggregation pathways of islet amyloid polypeptide.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Wei, Lei , Jiang, Ping , Xu, Weixin , Li, Hai , Zhang, Hua , Yan, Liang Yu , Chan-Park, Mary B. , Liu, Xue-Wei , Tang, Kai , Mu, Yuguang , Pervushin, Konstantin . 2554. "The molecular basis of distinct aggregation pathways of islet amyloid polypeptide".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Wei, Lei , Jiang, Ping , Xu, Weixin , Li, Hai , Zhang, Hua , Yan, Liang Yu , Chan-Park, Mary B. , Liu, Xue-Wei , Tang, Kai , Mu, Yuguang , Pervushin, Konstantin . "The molecular basis of distinct aggregation pathways of islet amyloid polypeptide."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2554. Print.
Wei, Lei , Jiang, Ping , Xu, Weixin , Li, Hai , Zhang, Hua , Yan, Liang Yu , Chan-Park, Mary B. , Liu, Xue-Wei , Tang, Kai , Mu, Yuguang , Pervushin, Konstantin . The molecular basis of distinct aggregation pathways of islet amyloid polypeptide. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2554.