9BI3
Crystal structure of macrocycle containing Abeta17-23 (LVF(a-Me-F)AED) and Abeta30-36 (AIIGL(ORN)V)
This is a non-PDB format compatible entry.
Summary for 9BI3
| Entry DOI | 10.2210/pdb9bi3/pdb |
| Descriptor | ORN-LEU-VAL-AMF-PHE-ALA-GLU-ASP-ORN-ALA-ILE-ILE-GLY-LEU-ORN-VAL (2 entities in total) |
| Functional Keywords | macrocyclic peptide, beta-hairpin, oligomer, de novo protein |
| Biological source | Homo sapiens |
| Total number of polymer chains | 2 |
| Total formula weight | 3526.26 |
| Authors | Samdin, T.D.,Kreutzer, A.G.,Wierzbicki, M.,Nowick, J.S. (deposition date: 2024-04-22, release date: 2025-03-05) |
| Primary citation | Samdin, T.D.,Kreutzer, A.G.,Sahrai, V.,Wierzbicki, M.,Nowick, J.S. alpha-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a beta-Hairpin Peptide Derived from A beta. J.Org.Chem., 90:394-400, 2025 Cited by PubMed Abstract: The assembly of the β-amyloid peptide Aβ into toxic oligomers plays a significant role in the neurodegeneration associated with the pathogenesis of Alzheimer's disease. Our laboratory has developed -methylation as a tool to enable X-ray crystallographic studies of oligomers formed by macrocyclic β-hairpin peptides derived from Aβ. In this investigation, we set out to determine whether α-methylation could be used as an alternative to -methylation in studying the oligomerization of a β-hairpin peptide derived from Aβ. α-Methylation permits the crystallographic assembly of a triangular trimer and ball-shaped dodecamer, resembling assemblies formed by the -methylated homolog. Subtle differences are observed in the conformation of the α-methylated peptide when compared to the -methylated homolog. Notably, α-methylation appears to promote a flatter and more extended β-sheet conformation than that of -methylated β-sheets or a typical unmodified β-sheet. α-Methylation provides an alternative to -methylation in X-ray crystallographic studies of oligomers formed by peptides derived from Aβ, with the attractive feature of preserving NH hydrogen-bond donors along the peptide backbone. PubMed: 39689228DOI: 10.1021/acs.joc.4c02344 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1 Å) |
Structure validation
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