Office of Research Amyloids - Office of Research



The Challenge

Harness the unique abilities of amyloid proteins to self-assemble and modify them slightly so they can grow nanometer scale particles capable of carrying out useful functions when collectively brought together in these amyloid ensembles.


Why It Is Important

The “amyloid” proteins are most known for the damage they do in unintended accumulations which can lead to such diseases as Alzheimer’s, Mad Cow, or Type II Diabetes. In the end, these proteins collect into one dimensional, nearly crystalline structures called “fibrils” which can be very long and are robust against exposure from high temperature, sunlight, and other extreme conditions.  Indeed, some organisms have evolved mechanisms for employing these accumulated proteins in useful means, such as one component of spider silk, and the stocks of lacewing eggs.

Our Approach

Notably, we hope to develop ways to generate photovoltaic devices with aligned nanoparticle rods, and thermoelectric refrigerant/heating devices with aligned wiring and materials.  We also want to examine whether the intrinsic amyloid structures bacteria and yeast employ in biocolony formation can be modified to template growth of photocatalytic materials that can break down environmental contaminants or potentially produce solar fuels.

Impacts & Highlights

  • The ANSWER team has succeeded in synthesizing two different designed beta solenoid fibrils, one with 2 sides, and one with 3 sides, and has preliminary evidence for lateral assembly of the 3 sided fibril, a crucial step towards building two dimensional protein templates for nanomaterials
  • Most significant achievement has been the design and synthesis of several modified (from wild type) BSP sequences which assemble into amyloid fibrils that appear to have the right characteristics
  • Demonstrated in principle control of length and twist, and made significant progress on design of lateral assembly with specificity
  • Initiated design of photovoltaics and thermoelectrics
  • Cox-Singh group has developed approaches to measure twist, twist moduli, and bending moduli for simulated fibrils of BSPs
  • Robert Hayre, postdoc in our group, implemented a suggestion by Niels Gronbech-Jensen and Oded Farago at Davis for improving the treatment of thermal noise included in molecular dynamics simulations. He also developed an adaptive box for simulation of long biomolecules.
  • Created the startup company Protein Architects Inc to facilitate development of the teams IP into potential products (April 2015)
  • Biologically Enabled Self Assembly Workshop was co-sponsored by the Institute for Complex Adaptive Matter and Florida A&M University; co-organized with Mogus Mochena from Florida A&M University:


Daniel Cox Professor of Physics
Xi Chen Professor of Chemistry
Joshua Hihath Assistant Professor of Electrical & Computer Engineering
Gang-yu Liu Professor of Chemistry
Ted Powers Professor of Molecular & Cellular Biology
Rajiv Singh Professor of Physics
Michael Toney Professor of Chemistry
Gergely Zimanyi Professor of Physics
Arpad Karsai Assistant Project Scientist of Chemistry
Krishna Ravikumar Postdoc of Physics
Qiang Fu Postdoc of Electrical & Computer Engineering
Zeyu Peng Postdoc of Chemistry
Maria del Peralta Graduate Student of Chemistry
Alice Ngo Graduate Student of Chemistry
Fernanda Banoni Graduate Student of Chemistry
Luman Qu Graduate Student of Physics
Jiali Zhang Graduate Student of Chemistry
Wei-Feng Len Graduate Student of Chemistry
Amanda Parker Graduate Student of Physics
Shengqiao Luo Undergraduate Student of Physics
Nima Mirzaee Undergraduate Student of Physics and Biomedical Engineering
Catherine Sierra Undergraduate Student of Pharmaceutical Chemistry
Kai Fong Undergraduate Student of Chemistry
Lai Chan Undergraduate Student of Neurobiology, Physiology, & Behavior

For more information on this program, please contact Christine Parks