Human Albumin Impairs Amyloid β-peptide Fibrillation Through its C-terminus: From docking Modeling to Protection Against Neurotoxicity in Alzheimer's disease.
AD, Alzheimer's disease
APP, amyloid precursor protein
Albumin
Alzheimer's disease
Amyloid
Aß, Amyloid-ß peptide
CD, Circular dichroism
CSF, cerebrospinal fluid
CTerm, albumin C-terminus
Docking
HPLC, high performance liquid chromatography
LC-MS, Liquid chromatography-mass spectrometry
MTT, 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
NMR, nuclear magnetic resonance
PBS, phosphate-buffered saline
PDB, Protein Data Bank
PPI, protein-protein interactions
SDS, sodium dodecyl sulfate
TEM, transmission electron microscopy
TFA, trifluoroacetic acid
UV, ultraviolet
fAβ1–42, HiLyte Fluor488 labelled human Aβ1–42
β-Sheet
Journal
Computational and structural biotechnology journal
ISSN: 2001-0370
Titre abrégé: Comput Struct Biotechnol J
Pays: Netherlands
ID NLM: 101585369
Informations de publication
Date de publication:
2019
2019
Historique:
received:
18
01
2019
revised:
03
06
2019
accepted:
13
06
2019
entrez:
31
7
2019
pubmed:
31
7
2019
medline:
31
7
2019
Statut:
epublish
Résumé
Alzheimer's disease (AD) is a neurodegenerative process characterized by the accumulation of extracellular deposits of amyloid β-peptide (Aβ), which induces neuronal death. Monomeric Aβ is not toxic but tends to aggregate into β-sheets that are neurotoxic. Therefore to prevent or delay AD onset and progression one of the main therapeutic approaches would be to impair Aβ assembly into oligomers and fibrils and to promote disaggregation of the preformed aggregate. Albumin is the most abundant protein in the cerebrospinal fluid and it was reported to bind Aβ impeding its aggregation. In a previous work we identified a 35-residue sequence of clusterin, a well-known protein that binds Aβ, that is highly similar to the C-terminus (CTerm) of albumin. In this work, the docking experiments show that the average binding free energy of the CTerm-Aβ
Identifiants
pubmed: 31360335
doi: 10.1016/j.csbj.2019.06.017
pii: S2001-0370(19)30018-2
pmc: PMC6639691
doi:
Types de publication
Journal Article
Langues
eng
Pagination
963-971Déclaration de conflit d'intérêts
None.
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