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Updated: Jul 6, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Cleavage agents for soluble oligomers of human islet amyloid polypeptide
Junghun Suh1, Woo Suk Chei, Tae Yeon Lee
1Department of Chemistry, Seoul National University, Seoul, 151-747, South Korea. jhsuh@snu.ac.kr
Abstract:
Soluble oligomers of human islet amyloid polypeptide (h-IAPP) are implicated in the initiation of beta-cell apoptosis leading to type 2 diabetes mellitus (T2DM). Cleavage of the h-IAPP included in an oligomer may provide a novel method for reducing the level of h-IAPP oligomers, offering a new therapeutic option for T2DM. From the combinatorial library of triazine derivatives prepared by exploiting the Co(III) complex of cyclen as the cleavage center for peptide bonds, eight compounds were selected as cleavage agents for oligomers of h-IAPP. After reaction with cleavage agents for 36 h at 37 degrees C and pH 7.50, up to 20 mol% of h-IAPP (initial concentration: 4.0 microM) was cleaved, although the target oligomers existed as transient species. Considerable activity was manifested at agent concentrations as low as 100 nM.
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