4.8 Article

Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.1416690112

Keywords

functional amyloid material; peptide self-assembly; nanosheet; retrovirus transduction; beta-amyloid

Funding

  1. 1000 Talents Program of China
  2. State High-Tech Development Plan (the 863 Program) Award [2015AA020907]
  3. National Natural Science Foundation (NSF) of China [31470748]
  4. China Postdoctoral Science Foundation [2014M560366, 2014T70446]
  5. National Basic Research Program of China (973 Program) [2013CB932801]
  6. NSF of China [11274334, 91227102, 11274075]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available