guest ::
| Home > Publications database > β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor |
| Home > Publications database > β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor |
| Journal Article | FZJ-2016-06321 |
; ; ; ; ; ;
2016
Nature Publishing Group
London
This record in other databases: 
Please use a persistent id in citations: http://hdl.handle.net/2128/12866 doi:10.1038/srep33474
Abstract: In type 2 diabetes, the formation of islet amyloid consisting of islet amyloid polypeptide (IAPP) isassociated with reduction in β-cell mass and contributes to the failure of islet cell transplantation.Rational design of inhibitors of IAPP amyloid formation has therapeutic potential, but is hampered bythe lack of structural information on inhibitor complexes of the conformationally flexible, aggregationproneIAPP. Here we characterize a β-hairpin conformation of IAPP in complex with the engineeredbinding protein β-wrapin HI18. The β-strands correspond to two amyloidogenic motifs, 12-LANFLVH-18and 22-NFGAILS-28, which are connected by a turn established around Ser-20. Besides backbonehydrogen bonding, the IAPP:HI18 interaction surface is dominated by non-polar contacts involvinghydrophobic side chains of the IAPP β-strands. Apart from monomers, HI18 binds oligomers and fibrilsand inhibits IAPP aggregation and toxicity at low substoichiometric concentrations. The IAPP β-hairpincan serve as a molecular recognition motif enabling control of IAPP aggregation.
; 
; 
; 
; BIOSIS Previews ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; IF >= 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record
|
The record appears in these collections: |
PDF
PDF (PDFA)