Control of Amyloid Beta Peptide Self-Assembly Public

Abstract

The self-assembly of amyloid beta peptide forms plaque, some of which cause Alzheimer's disease. Assembly depends on the tissue environment. The Dutch mutant model, Aβ(16-22) E22Q, reveals clear progressive stages of assembly, from particle formation to para-crystalline mutation, that can now be used to control the various stages of assembly. Changes in the dielectric of the media, the shear forces on the assemblies, and site-specific substitutions now provide insight into strand orientation, strand registry, fiber twisting and bundling, and ribbon helicity. An initial structural code is now emerging where the rate of progression through various intermediates and the final architecture of the assembly can be controlled to construct well-defined mesoscale materials.

Table of Contents

Abstract 1

Introduction 1

Materials and Methods 2

1. Peptide synthesis and purification 2

2. Fibril assembly 2

3. Sample monitoring 3

Results and Discussion 3

1. E22Q Salt Project 3

1.1. Oligomerization and Nucleation at Particle Phase 3

1.2. Structural Mutation during Propagation 5

2. E22Q Agitation Project 6

3. L17Q Project 8

3.1 Preliminary study revealed the ¹²C-¹³C peak coupling pattern of the L17Q IR spectra 8

3.2. Comparing L17Q Assembly in pH2 vs pH7 8

Conclusion 10

Reference 10

About this Honors Thesis

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School	Emory College
Department	Chemistry
Degree	BS
Submission	Honors Thesis
Language	English
Research Field	Chemistry, Biochemistry Chemistry, General
Mot-clé	Aβ peptide assembly Shearing force Glutamine hydrogen bonding Media dielectric
Committee Chair / Thesis Advisor	Lynn, David, Emory University
Committee Members	Deal, Roger, Emory University Soria, Jose, Emory University

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