Molecular modeling of apoE in complexes with Alzheimer's amyloid-β fibrils from human brain suggests a structural basis for apolipoprotein co-deposition with amyloids.
Amphipathic apolipoprotein α-helices
Amyloid signature proteins
Atomic structures
Cryptic binding sites
Exposed hydrophobic surfaces
Fibril polymorphs
Journal
bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
06 Aug 2023
06 Aug 2023
Historique:
pubmed:
14
8
2023
medline:
14
8
2023
entrez:
14
8
2023
Statut:
epublish
Résumé
Apolipoproteins co-deposit with amyloids, yet apolipoprotein-amyloid interactions are enigmatic. To understand how apoE interacts with Alzheimer's amyloid-β (Aβ) peptide in fibrillary deposits, the NMR structure of full-length human apoE was docked to four structures of patient-derived Aβ
Identifiants
pubmed: 37577501
doi: 10.1101/2023.08.04.551703
pmc: PMC10418262
pii:
doi:
Types de publication
Preprint
Langues
eng
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM067260
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM135158
Pays : United States
Organisme : NHLBI NIH HHS
ID : R01 HL036153
Pays : United States
Organisme : NIDDK NIH HHS
ID : T32 DK007201
Pays : United States
Commentaires et corrections
Type : UpdateIn
Déclaration de conflit d'intérêts
Disclosure statement. All authors have no financial or any other conflicts of interests to disclose.