Purpurin modulates Tau-derived VQIVYK fibrillization and ameliorates Alzheimer's disease-like symptoms in animal model.


Journal

Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402

Informations de publication

Date de publication:
Jul 2020
Historique:
received: 10 03 2019
accepted: 19 09 2019
revised: 11 08 2019
pubmed: 29 9 2019
medline: 11 7 2020
entrez: 29 9 2019
Statut: ppublish

Résumé

Neurofibrillary tangles of the Tau protein and plaques of the amyloid β peptide are hallmarks of Alzheimer's disease (AD), which is characterized by the conversion of monomeric proteins/peptides into misfolded β-sheet rich fibrils. Halting the fibrillation process and disrupting the existing aggregates are key challenges for AD drug development. Previously, we performed in vitro high-throughput screening for the identification of potent inhibitors of Tau aggregation using a proxy model, a highly aggregation-prone hexapeptide fragment

Identifiants

pubmed: 31562564
doi: 10.1007/s00018-019-03312-0
pii: 10.1007/s00018-019-03312-0
doi:

Substances chimiques

Amyloid beta-Peptides 0
Anthraquinones 0
Oligopeptides 0
Peptide Fragments 0
Protein Aggregates 0
Repressor Proteins 0
tau Proteins 0
tau hexapeptide PHF6 0
purpurin anthraquinone L1GT81LS6N

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

2795-2813

Auteurs

Guru Krishnakumar Viswanathan (GK)

Department of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.

Dana Shwartz (D)

Department of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.

Yelena Losev (Y)

Department of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.

Elad Arad (E)

Ilse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.
Department of Chemistry, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.

Chen Shemesh (C)

The Joseph Sagol Neuroscience Center, Sheba Medical Center, Tel Hashomer, 52621, Ramat Gan, Israel.

Edward Pichinuk (E)

Blavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.

Hamutal Engel (H)

Blavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.

Avi Raveh (A)

Blavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.

Raz Jelinek (R)

Ilse Katz Institute (IKI) for Nanoscale Science and Technology, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.
Department of Chemistry, Ben Gurion University of the Negev, 8410501, Beer Sheva, Israel.

Itzik Cooper (I)

The Joseph Sagol Neuroscience Center, Sheba Medical Center, Tel Hashomer, 52621, Ramat Gan, Israel.
Interdisciplinary Center Herzliya, Herzliya, Israel.

Fabien Gosselet (F)

Blood-Brain Barrier Laboratory (LBHE), Université d'Artois, Lens, France.

Ehud Gazit (E)

Department of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel.
Blavatnik Center for Drug Discovery, Tel-Aviv University, 69978, Tel Aviv, Israel.

Daniel Segal (D)

Department of Molecular Microbiology and Biotechnology, School of Molecular Cell Biology and Biotechnology, Tel-Aviv University, 69978, Tel Aviv, Israel. dsegal@post.tau.ac.il.
The Interdisciplinary Sagol School of Neurosciences, Tel-Aviv University, 69978, Tel Aviv, Israel. dsegal@post.tau.ac.il.

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Classifications MeSH