Academic Field

Chemistry, Chemical Engineering

Faculty Mentor Name

Dr. Kazushige Yokoyama

Presentation Type

Poster Presentation

Abstract

The fiber formation of amyloid beta peptides is known to be an essential step of fibrillogenesis, the hallmark mechanism of Alzheimer's disease. One type of amyloid beta which is critically important in the mechanism of Alzheimer’s disease is a hydrophilic amyloid beta of sequences 1-40. A fluorescein-attached amyloid beta monomer (Faβ1-40) of this sequence was used to probe the conformational change of the peptide into its oligomeric formation. The folded and unfolded conformations of the monomer were induced by fluctuating the pH environment between 10 and 4, respectively. This was studied at an interfacial environment using gold colloidal surfaces, ranging between 10 nm and 100 nm in diameter. The bonding dynamics for the Faβ1-40 was determined from fluorescence decay times. Faster dynamics were observed in acidic environments as well as in the presence of the larger gold colloids due to an enhancement in fluorescence from the peptide.

Keywords

Alzheimer's disease, amyloid beta peptides, gold colloids

Start Date

10-4-2015 11:15 AM

End Date

10-4-2015 12:00 PM

Location

SERC House of Fields

Share

COinS
 
Apr 10th, 11:15 AM Apr 10th, 12:00 PM

Reversible Self-Assembly of Fluorescein Amyloid Beta Peptides over Gold Colloids

SERC House of Fields

The fiber formation of amyloid beta peptides is known to be an essential step of fibrillogenesis, the hallmark mechanism of Alzheimer's disease. One type of amyloid beta which is critically important in the mechanism of Alzheimer’s disease is a hydrophilic amyloid beta of sequences 1-40. A fluorescein-attached amyloid beta monomer (Faβ1-40) of this sequence was used to probe the conformational change of the peptide into its oligomeric formation. The folded and unfolded conformations of the monomer were induced by fluctuating the pH environment between 10 and 4, respectively. This was studied at an interfacial environment using gold colloidal surfaces, ranging between 10 nm and 100 nm in diameter. The bonding dynamics for the Faβ1-40 was determined from fluorescence decay times. Faster dynamics were observed in acidic environments as well as in the presence of the larger gold colloids due to an enhancement in fluorescence from the peptide.