1QWP
NMR analysis of 25-35 fragment of beta amyloid peptide
Summary for 1QWP
| Entry DOI | 10.2210/pdb1qwp/pdb |
| Related | 1IYT |
| Descriptor | 11-mer peptide from Amyloid beta A4 protein (1 entity in total) |
| Functional Keywords | amyloid beta peptide- kink structure, protein binding |
| Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
| Total number of polymer chains | 1 |
| Total formula weight | 1061.28 |
| Authors | D'Ursi, A.M.,Armenante, M.R.,Guerrini, R.,Salvadori, S.,Sorrentino, G.,Picone, D. (deposition date: 2003-09-03, release date: 2004-09-14, Last modification date: 2024-05-29) |
| Primary citation | D'Ursi, A.M.,Armenante, M.R.,Guerrini, R.,Salvadori, S.,Sorrentino, G.,Picone, D. Solution structure of amyloid beta-peptide (25-35) in different media J.Med.Chem., 47:4231-4238, 2004 Cited by PubMed Abstract: 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. PubMed: 15293994DOI: 10.1021/jm040773o PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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