1qwp
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1iyt|1IYT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwp OCA], [http://www.ebi.ac.uk/pdbsum/1qwp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qwp RCSB]</span> | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Alzheimer disease-1, APP-related OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=104760 104760]], Amyloidosis, cerebroarterial, Dutch type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=104760 104760]], Amyloidosis, cerebroarterial, Iowa type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=104760 104760]], Blood group, P system OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607922 607922]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: amyloid beta peptide- kink structure]] | [[Category: amyloid beta peptide- kink structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:02 2008'' |
Revision as of 20:20, 30 March 2008
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| Related: | 1IYT
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR analysis of 25-35 fragment of beta amyloid peptide
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.
About this Structure
1QWP 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
Page seeded by OCA on Sun Mar 30 23:20:02 2008
