Structure-based design of functional amyloid materials

J Am Chem Soc. 2014 Dec 31;136(52):18044-51. doi: 10.1021/ja509648u. Epub 2014 Dec 19.

Abstract

Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of biological nanomaterials. Here we introduce a method that utilizes the atomic structures of amyloid peptides, to design materials with versatile applications. As a model application, we designed amyloid fibers capable of capturing carbon dioxide from flue gas, to address the global problem of excess anthropogenic carbon dioxide. By measuring dynamic separation of carbon dioxide from nitrogen, we show that fibers with designed amino acid sequences double the carbon dioxide binding capacity of the previously reported fiber formed by VQIVYK from Tau protein. In a second application, we designed fibers that facilitate retroviral gene transfer. By measuring lentiviral transduction, we show that designed fibers exceed the efficiency of polybrene, a commonly used enhancer of transduction. The same procedures can be adapted to the design of countless other amyloid materials with a variety of properties and uses.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry*
  • Carbon Dioxide / chemistry
  • Carbon Dioxide / isolation & purification
  • Drug Design*
  • HEK293 Cells
  • HIV-1 / genetics
  • Humans
  • Models, Molecular
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology
  • Protein Structure, Secondary
  • Transduction, Genetic

Substances

  • Amyloid
  • Peptide Fragments
  • Carbon Dioxide