Inhibition of tau-derived hexapeptide aggregation and toxicity by a self-assembled cyclic d,l-α-peptide conformational inhibitor

A Belostozky; M Richman; E Lisniansky; A Tovchygrechko; J H Chill; S Rahimipour

doi:10.1039/c8cc01233d

Inhibition of tau-derived hexapeptide aggregation and toxicity by a self-assembled cyclic d,l-α-peptide conformational inhibitor

Chem Commun (Camb). 2018 Jun 8;54(47):5980-5983. doi: 10.1039/c8cc01233d.

Authors

A Belostozky¹, M Richman, E Lisniansky, A Tovchygrechko, J H Chill, S Rahimipour

Affiliation

¹ Department of Chemistry, Bar-Ilan University, Ramat-Gan 5290002, Israel. [email protected].

PMID: 29790502
DOI: 10.1039/c8cc01233d

Abstract

Aggregation and accumulation of amyloid β and tau proteins to plaques and neurofibrillary tangles are the key pathogenic events in Alzheimer's disease. Here, we studied the capability of the cyclic d,l-α-peptide CP-2 as a conformational inhibitor of different amyloids to cross-interact with tau-derived AcPHF6 peptide and inhibit its aggregation, membrane perturbation and toxicity.

MeSH terms

Amyloidogenic Proteins / antagonists & inhibitors*
Amyloidogenic Proteins / chemistry
Amyloidogenic Proteins / metabolism
Animals
Heparin / metabolism
Oligopeptides / antagonists & inhibitors*
Oligopeptides / chemistry
Oligopeptides / metabolism
PC12 Cells
Peptides, Cyclic / chemistry
Peptides, Cyclic / pharmacology*
Peptides, Cyclic / toxicity
Protein Multimerization
Protein Structure, Secondary
Rats
Stereoisomerism

Substances

Amyloidogenic Proteins
Oligopeptides
Peptides, Cyclic
acetyl-valyl-glutaminyl-isoleucyl-valyl-tyrosyl-lysinamide
Heparin