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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Grentz, Wolfgang Kav, Batuhan Dobson, Christopher M. Dean, James Müller, Thomas Michaels, Thomas C. T. Terentjev, Eugene M. Garcia, Gonzalo A. Knowles, Tuomas P. J. Herling, Therese W. Gang, Hongze Shimanovich, Ulyana |
| Description | Author Affiliation: Herling TW ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Garcia GA ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Michaels TC ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Grentz W ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Dean J ( Department of Materials Science and Metallurgy, University of Cambridge, Cambridge CB3 0FS, United Kingdom); Shimanovich U ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Gang H ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Müller T ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Kav B ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Terentjev EM ( Cavendish Laboratory, University of Cambridge, Cambridge CB3 0HE, United Kingdom.); Dobson CM ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); Knowles TP ( Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom); |
| Abstract | The generation of mechanical forces are central to a wide range of vital biological processes, including the function of the cytoskeleton. Although the forces emerging from the polymerization of native proteins have been studied in detail, the potential for force generation by aberrant protein polymerization has not yet been explored. Here, we show that the growth of amyloid fibrils, archetypical aberrant protein polymers, is capable of unleashing mechanical forces on the piconewton scale for individual filaments. We apply microfluidic techniques to measure the forces released by amyloid growth for two systems: insulin and lysozyme. The level of force measured for amyloid growth in both systems is comparable to that observed for actin and tubulin, systems that have evolved to generate force during their native functions and, unlike amyloid growth, rely on the input of external energy in the form of nucleotide hydrolysis for maximum force generation. Furthermore, we find that the power density released from growing amyloid fibrils is comparable to that of high-performance synthetic polymer actuators. These findings highlight the potential of amyloid structures as active materials and shed light on the criteria for regulation and reversibility that guide molecular evolution of functional polymers. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 31 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amyloid Chemistry Protein Aggregates Animals Biomechanical Phenomena Microfluidics Muramidase Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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