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

  1. Cong Liua,2
  1. aInterdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China;
  2. bState Key Laboratory of Surface Physics, Key Laboratory for Computational Physical Sciences (Ministry of Education), Department of Physics, Fudan University, Shanghai 200433, China;
  3. cNational Center for Protein Science (Shanghai), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 201210, China; and
  4. dLaboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China

  1. Edited by Michael L. Klein, Temple University, Philadelphia, PA, and approved February 3, 2015 (received for review August 31, 2014)

Significance

Many proteins enter the amyloid state, which is associated with human diseases and is also involved in many biological events. Amyloid formed by various proteins has a uniform “cross-β” structure with protein units stacking repetitively into fibrils. This unique structure brings amyloid favorable mechanical and chemical properties, and inspires the exploration of amyloid as a novel class of bionanomaterials. On the other hand, the uniform fibrillar structure limits the application of amyloid materials for a diverse function. This paper illustrates our discovery, structure characterization, design, and application of an amyloid-based structure, termed “amyloid-like nanosheet.” This nanosheet enriches the architectures of amyloid materials and will aid researchers in designing and investigating amyloid with new functions.

Abstract

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.

Footnotes

  • ↵1B.D. and D.L. contributed equally to this work.

  • ↵2To whom correspondence may be addressed. Email: liulab{at}sioc.ac.cn, ghwei{at}fudan.edu.cn, or zhangyi{at}sinap.ac.cn.

  • Author contributions: B.D., D.L., and C.L. designed research; B.D., D.L., W.X., F.L., X.Z., and M.Z. performed research; W.X., F.L., M.C., J.H., W.W., G.W., and Y.Z. contributed new reagents/analytic tools; B.D., D.L., and C.L. analyzed data; and D.L. and C.L. wrote the paper.

  • The authors declare no conflict of interest.

  • This article is a PNAS Direct Submission.

  • This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1416690112/-/DCSupplemental.

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