Chaperon-mediated single molecular approach toward modulating Abeta peptide aggregation

We report here a single molecular approach using chaperone-like molecular modulators for modulating the aggregation behavior of a vital analogue of beta-amyloid peptide (Abeta) by using scanning tunneling microscopy. The molecular structures of the beta-sheets for Abeta33-42 peptide are revealed, which are keen to the aggregation of Abeta42 relating to Alzheimer's disease. It was identified that the introduction of chaperone-like modulators could regulate the assembling behavior of the peptide at molecular level. Furthermore, the modulators could also significantly accelerate the aggregation of the peptide in aqueous solution as revealed by light scattering studies. These observations of the molecular modulator effect in peptide assemblies could provide a novel approach toward modulating Abeta peptide aggregations.

Medienart:

E-Artikel

Erscheinungsjahr:

2009

Erschienen:

2009

Enthalten in:

Zur Gesamtaufnahme - volume:9

Enthalten in:

Nano letters - 9(2009), 12 vom: 19. Dez., Seite 4066-72

Sprache:

Englisch

Beteiligte Personen:

Liu, Lei [VerfasserIn]
Zhang, Lan [VerfasserIn]
Mao, Xiaobo [VerfasserIn]
Niu, Lin [VerfasserIn]
Yang, Yanlian [VerfasserIn]
Wang, Chen [VerfasserIn]

Links:

Volltext

Themen:

Amyloid beta-Peptides
Journal Article
Molecular Chaperones
Multiprotein Complexes
Research Support, Non-U.S. Gov't

Anmerkungen:

Date Completed 22.02.2010

Date Revised 30.09.2020

published: Print

Citation Status MEDLINE

doi:

10.1021/nl902256b

funding:

Förderinstitution / Projekttitel:

PPN (Katalog-ID):

NLM192177486