Structural highlights
Publication Abstract from PubMed
The assembly of the beta-amyloid peptide, Abeta, into soluble oligomers is associated with neurodegeneration in Alzheimer's disease. The Abeta oligomers are thought to be composed of beta-hairpins. Here, the effect of shifting the residue pairing of the beta-hairpins on the structures of the oligomers that form is explored through X-ray crystallography. Three residue pairings were investigated using constrained macrocyclic beta-hairpins in which Abeta30-36 is juxtaposed with Abeta17-23, Abeta16-22, and Abeta15-21. The Abeta16-22-Abeta30-36 pairing forms a compact ball-shaped dodecamer composed of fused triangular trimers. This dodecamer may help explain the structures of the trimers and dodecamers formed by full-length Abeta.
X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Abeta16-36.,Salveson PJ, Spencer RK, Kreutzer AG, Nowick JS Org Lett. 2017 Jul 7;19(13):3462-3465. doi: 10.1021/acs.orglett.7b01445. Epub, 2017 Jun 15. PMID:28683555[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Salveson PJ, Spencer RK, Kreutzer AG, Nowick JS. X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from Abeta16-36. Org Lett. 2017 Jul 7;19(13):3462-3465. doi: 10.1021/acs.orglett.7b01445. Epub, 2017 Jun 15. PMID:28683555 doi:http://dx.doi.org/10.1021/acs.orglett.7b01445
