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

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

Department of Chemistry

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	5980-5983
Number of pages	4
Journal	Chemical Communications
Volume	54
Issue number	47
DOIs	https://doi.org/10.1039/c8cc01233d
State	Published - 8 Jun 2018

All Science Journal Classification (ASJC) codes

Catalysis
Electronic, Optical and Magnetic Materials
Ceramics and Composites
General Chemistry
Surfaces, Coatings and Films
Metals and Alloys
Materials Chemistry

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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.",

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AU - Belostozky, A.

AU - Richman, M.

AU - Lisniansky, E.

AU - Tovchygrechko, A.

AU - Chill, J. H.

AU - Rahimipour, S.

PY - 2018/6/8

Y1 - 2018/6/8

N2 - 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.

AB - 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.

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U2 - 10.1039/c8cc01233d

DO - 10.1039/c8cc01233d

M3 - مقالة

C2 - 29790502

SN - 1359-7345

VL - 54

SP - 5980

EP - 5983

JO - Chemical Communications

JF - Chemical Communications

IS - 47

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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