Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	An O-glycopeptide participates in the formation of distinct Aβ fibril structures and attenuates Aβ neurotoxicity.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 5815, Year 2025
Publish date	Jul 1, 2025
Authors	Qijia Wei / Dangliang Liu / Wencheng Xia / Fengzhang Wang / Lu Huang / Jun Zhang / Xiaoya Wang / Zhongxin Xu / Changdong He / Wenzhe Li / Xiaomeng Shi / Chu Wang / Yuan Liu / Cong Liu / Suwei Dong /
PubMed Abstract	The self-assembly of biomolecules through noncovalent interactions is critical in both physiological and pathological processes, as exemplified by the assembly of amyloid β peptide (Aβ) into ...The self-assembly of biomolecules through noncovalent interactions is critical in both physiological and pathological processes, as exemplified by the assembly of amyloid β peptide (Aβ) into oligomers or fibrils in Alzheimer's disease (AD). Developing molecules that can modulate this assembly process holds significant mechanistic and therapeutic potential. In this study, we identified glycopeptides as a class of protein aggregation modulators, showing that β-N-acetylgalactosamine (β-GalNAc)-modified Aβ promotes Aβ fibrillation while reducing its toxic oligomers. Using biochemical assays, cryo-EM, and molecular dynamics simulations, we demonstrated that β-GalNAc-modified Aβ coassembles with Aβ, forming unique fibril structures stabilized by both hydrophobic interactions and an organized hydrogen bond network facilitated by the glycopeptide. Importantly, β-GalNAc-modified Aβ can alleviate the neurotoxicity of Aβ in neuronal cells and an AD male mouse model. These findings underscore the potential of glycopeptides in regulating amyloid aggregation and provide structural insights for designing molecules targeting amyloid-related pathologies.
External links	Nat Commun / PubMed:40593714 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.6 - 3.7 Å
Structure data	61944 9k0d EMDB-61944, PDB-9k0d: Cryo-EM structure of Amyloid-beta42-4b polymorph 1 Method: EM (helical sym.) / Resolution: 2.6 Å 61945 9k0e EMDB-61945, PDB-9k0e: Cryo-EM structure of Amyloid-beta42-4b polymorph 2 Method: EM (helical sym.) / Resolution: 2.8 Å 61946 9k0f EMDB-61946, PDB-9k0f: Cryo-EM structure of Amyloid-beta42-4b polymorph 3 Method: EM (helical sym.) / Resolution: 2.8 Å EMDB-63403: Cryo-EM density map of Amyloid-beta42 WT Method: EM (helical sym.) / Resolution: 3.7 Å
Chemicals	ChemComp-HOH: WATER
Source	homo sapiens (human)
Keywords	MEMBRANE PROTEIN / helical fibril / amyloid-beta / PROTEIN FIBRIL