Related Experiment Video
Updated: May 4, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Internal and environmental effects on folding and dimerization of the Alzheimer's β amyloid peptide
Priya Anand1, Ulrich H E Hansmann1
1Department of Physics, Michigan Technological University, Houghton, MI 49931, USA.
Abstract:
Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease a turn between 21Ala and 30Ala, stabilized by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the Aβ peptide. In the present paper we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes effect folding and aggregation of the Aβ peptide.
Related Concept Videos
Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid Fibrils
Alzheimer Disease ll: Pathophysiology
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Alzheimer Disease l: Introduction

