Cleavage agents for soluble oligomers of human islet amyloid polypeptide
| Autor: | Sang Ho Yoo, Junghun Suh, Min Gyum Kim, Keunhong Jeong, Woo Suk Chei, Tae Yeon Lee, Jae Young Ahn |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Amyloid
endocrine system Amylin Cleavage (embryo) Biochemistry Oligomer Inorganic Chemistry chemistry.chemical_compound Hydrolysis Isomerism Cyclen Combinatorial Chemistry Techniques Peptide bond Triazine geography Amyloid beta-Peptides geography.geographical_feature_category Triazines Hydrogen-Ion Concentration Islet Peptide Fragments Islet Amyloid Polypeptide chemistry Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Indicators and Reagents Filtration |
| Zdroj: | JBIC Journal of Biological Inorganic Chemistry. 13:693-701 |
| ISSN: | 1432-1327 0949-8257 |
| DOI: | 10.1007/s00775-008-0354-y |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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