1qyt
From Proteopedia
(New page: 200px<br /> <applet load="1qyt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qyt" /> '''Solution structure of fragment (25-35) of b...) |
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'''Solution structure of fragment (25-35) of beta amyloid peptide in SDS micellar solution'''<br /> | '''Solution structure of fragment (25-35) of beta amyloid peptide in SDS micellar solution'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1QYT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: amyloid beta peptide- kink structure]] | [[Category: amyloid beta peptide- kink structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:46:24 2008'' |
Revision as of 14:46, 15 February 2008
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Solution structure of fragment (25-35) of beta amyloid peptide in SDS micellar solution
Contents |
Overview
The design of molecules able to interact with the amyloid peptides either, as inhibitors of fibril formation or as inhibitors of amyloid membrane, pore formation represents one of the most relevant approaches in the, development of anti-Alzheimer therapies. Abeta-(25-35), sequence, GSNKGAIIGLM, is a highly toxic synthetic derivative of amyloid, beta-peptides (Abeta-peptides), which forms fibrillary aggregates. Here, we report the NMR and CD investigation of Abeta-(25-35) in a, membrane-mimicking environment and in isotropic mixtures of water and, fluoro-alcohols to scan its conformational properties as a function of the, medium. The analysis of the 3D structures in the mentioned conditions, indicates a propensity of the peptide to behave as a typical transmembrane, helix in the lipidic environment. In media characterized by different, polarity, it loses the structural regularity at specific points of the, sequence as a function of the environment. Furthermore, a comparison with, the solution structure of full-length amyloid peptides suggests a role for, the 25-27 kink region, which appears to be a general feature of all, peptides under the solution conditions explored.
Disease
Known diseases associated with this structure: Alzheimer disease-1, APP-related OMIM:[104760], Amyloidosis, cerebroarterial, Dutch type OMIM:[104760], Amyloidosis, cerebroarterial, Iowa type OMIM:[104760], Blood group, P system OMIM:[607922]
About this Structure
1QYT is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure of amyloid beta-peptide (25-35) in different media., D'Ursi AM, Armenante MR, Guerrini R, Salvadori S, Sorrentino G, Picone D, J Med Chem. 2004 Aug 12;47(17):4231-8. PMID:15293994
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