This is an early access version, the complete PDF, HTML, and XML versions will be available soon.
Open AccessArticle
Surface Hydrophobicity Strongly Influences Adsorption and Conformation of Amyloid Beta Derived Peptides
by
David L. Cheung
David L. Cheung
David L Cheung received his PhD from the University of Durham. Following he performed postdoctoral a [...]
David L Cheung received his PhD from the University of Durham. Following he performed postdoctoral research at the University of Bielefeld and University of Warwick. Dr. Cheung is now a Lecturer in Biophysical Chemistry at the School of Chemistry University of Galway. Before this, Dr. Cheung was a Lecturer in Physical Chemistry in the Department of Pure and Applied Chemistry at the University of Strathclyde and a Leverhulme Trust Early Career Fellow in the Department of Chemistry and Centre for Scientific Computing, University of Warwick. He has published over 40 papers in peer-reviewed journals and made over thirty oral presentations to external research groups and at national and international conferences. His research focuses on the study of soft interfaces, such as those between different liquids (e.g. oil and water), membranes, or soft surfaces.
School of Biological and Chemical Sciences, University of Galway, University Road, H91 TK33 Galway, Ireland
Molecules 2024, 29(15), 3634; https://doi.org/10.3390/molecules29153634 (registering DOI)
Submission received: 14 June 2024
/
Revised: 19 July 2024
/
Accepted: 25 July 2024
/
Published: 31 July 2024
Abstract
The formation of amyloid fibrils is a common feature of many protein systems. It has implications in both health, as amyloid fibrils are implicated in over 30 degenerative diseases, and in the biological functions of proteins. Surfaces have long been known to affect the formation of fibrils but the specific effect depends on the details of both the surface and protein. Fully understanding the role of surfaces in fibrillization requires microscopic information on protein conformation on surfaces. In this paper replica exchange molecular dynamics simulation is used to investigate the model fibril forming protein, A(10–40) (a 31-residue segment of the amyloid-beta protein) on surfaces of different hydrophobicity. Similar to other proteins A(10–40) is found to adsorb strongly onto hydrophobic surfaces. It also adopts significantly different sets of conformations on hydrophobic and polar surfaces, as well as in bulk solution. On hydrophobic surfaces, it adopts partially helical structures, with the helices overlapping with beta-strand regions in the mature fibril. These may be helical intermediates on the fibril formation pathway, suggesting a mechanism for the enhanced fibril formation seen on hydrophobic surfaces.
Share and Cite
MDPI and ACS Style
Cheung, D.L.
Surface Hydrophobicity Strongly Influences Adsorption and Conformation of Amyloid Beta Derived Peptides. Molecules 2024, 29, 3634.
https://doi.org/10.3390/molecules29153634
AMA Style
Cheung DL.
Surface Hydrophobicity Strongly Influences Adsorption and Conformation of Amyloid Beta Derived Peptides. Molecules. 2024; 29(15):3634.
https://doi.org/10.3390/molecules29153634
Chicago/Turabian Style
Cheung, David L.
2024. "Surface Hydrophobicity Strongly Influences Adsorption and Conformation of Amyloid Beta Derived Peptides" Molecules 29, no. 15: 3634.
https://doi.org/10.3390/molecules29153634
Article Metrics
Article metric data becomes available approximately 24 hours after publication online.