Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 112, Issue 10, Pages 2996-3001Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1416690112
Keywords
functional amyloid material; peptide self-assembly; nanosheet; retrovirus transduction; beta-amyloid
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Funding
- 1000 Talents Program of China
- State High-Tech Development Plan (the 863 Program) Award [2015AA020907]
- National Natural Science Foundation (NSF) of China [31470748]
- China Postdoctoral Science Foundation [2014M560366, 2014T70446]
- National Basic Research Program of China (973 Program) [2013CB932801]
- NSF of China [11274334, 91227102, 11274075]
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Using and engineering amyloid as nanomaterials are blossoming trends in bionanotechnology. Here, we show our discovery of an amyloid structure, termed amyloid-like nanosheet, formed by a key amyloid-forming segment of Alzheimer's A beta. Combining multiple biophysical and computational approaches, we proposed a structural model for the nanosheet that is formed by stacking the amyloid fibril spines perpendicular to the fibril axis. We further used the nanosheet for laboratorial retroviral transduction enhancement and directly visualized the presence of virus on the nanosheet surface by electron microscopy. Furthermore, based on our structural model, we designed nanosheet-forming peptides with different functionalities, elucidating the potential of rational design for amyloid-based materials with novel architecture and function.
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