Stabilization of Monomeric Tau Protein by All D-Enantiomeric Peptide Ligands as Therapeutic Strategy for Alzheimer's Disease and Other Tauopathies.
Alzheimer’s disease
all D-enantiomeric peptides
mirror-image phage display
tau aggregation
tauopathies
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
21 Jan 2023
21 Jan 2023
Historique:
received:
24
11
2022
revised:
10
01
2023
accepted:
16
01
2023
entrez:
11
2
2023
pubmed:
12
2
2023
medline:
15
2
2023
Statut:
epublish
Résumé
Alzheimer's disease and other tauopathies are the world's leading causes of dementia and memory loss. These diseases are thought to be caused by the misfolding and aggregation of the intracellular tau protein, ultimately leading to neurodegeneration. The tau protein is involved in a multitude of different neurodegenerative diseases. During the onset of tauopathies, tau undergoes structural changes and posttranslational modifications and aggregates into amyloid fibrils that are able to spread with a prion-like behavior. Up to now, there is no therapeutic agent which effectively controls or reverses the disease. Most of the therapeutics that were developed and underwent clinical trials targeted misfolded or aggregated forms of tau. In the current manuscript, we present the selection and characterization of two all D-enantiomeric peptides that bind monomeric tau protein with a low nanomolar K
Identifiants
pubmed: 36768484
pii: ijms24032161
doi: 10.3390/ijms24032161
pmc: PMC9917023
pii:
doi:
Substances chimiques
tau Proteins
0
Amyloid
0
Peptides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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