1qwp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|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>
}}
}}
Line 14: Line 17:
==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.
- 
-
==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==
Line 32: Line 32:
[[Category: amyloid beta peptide- kink structure]]
[[Category: amyloid beta peptide- kink structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:43 2008''
+
''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


PDB ID 1qwp

Drag the structure with the mouse to rotate
Related: 1IYT


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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools