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Tunable assembly of amyloid-forming peptides into nanosheets as a retrovirus carrier
Author(s) -
Bin Dai,
Dan Li,
Wenhui Xi,
Fang Luo,
Xiang Zhang,
Man Zou,
Mi Cao,
Jun Hu,
Wenyuan Wang,
Guanghong Wei,
Yi Zhang,
Cong Liu
Publication year - 2015
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1416690112
Subject(s) - nanosheet , amyloid (mycology) , amyloid fibril , biophysics , nanomaterials , fibril , nanotechnology , materials science , nanobiotechnology , chemistry , amyloid β , biology , nanoparticle , medicine , pathology , inorganic chemistry , disease
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 Aβ. 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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