Journal
CHEMICAL COMMUNICATIONS
Volume 46, Issue 42, Pages 8023-8025Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c0cc02555k
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Funding
- National Natural Science Foundation of China [20825206, 90913003, 20091350914]
- Sino-German Center for Research Promotion [GZ561]
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Human islet amyloid polypeptide (hIAPP) deposit is the hallmark of type 2 diabetes pathology. Here, we report that apo-cyclen, attached to a specific hIAPP recognition motif (NYGAIL), captured copper ions and became proteolytically active. This cyclen-NYGAIL-copper complex was able to interfere with hIAPP aggregation and cleave hIAPP. These activities rescued INS-1 cells from hIAPP induced cytotoxicity.
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