1. Academic Validation
  2. Rigid helical-like assemblies from a self-aggregating tripeptide

Rigid helical-like assemblies from a self-aggregating tripeptide

  • Nat Mater. 2019 May;18(5):503-509. doi: 10.1038/s41563-019-0343-2.
Santu Bera 1 Sudipta Mondal 1 Bin Xue 2 Linda J W Shimon 3 Yi Cao 2 Ehud Gazit 4
Affiliations

Affiliations

  • 1 Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Israel.
  • 2 Collaborative Innovation Center of Advanced Microstructures, National Laboratory of Solid State Microstructure, Department of Physics, Nanjing University, Nanjing, Jiangsu, China.
  • 3 Department of Chemical Research Support, Weizmann Institute of Science, Rehovot, Israel.
  • 4 Department of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv, Israel. ehudg@post.tau.ac.il.
Abstract

The structural versatility, biocompatibility and dynamic range of the mechanical properties of protein Materials have been explored in functional biomaterials for a wide array of biotechnology applications. Typically, such Materials are made from self-assembled Peptides with a predominant β-sheet structure, a common structural motif in silk and amyloid fibrils. However, collagen, the most abundant protein in mammals, is based on a helical arrangement. Here we show that Pro-Phe-Phe, the most aggregation-prone tripeptide of natural Amino acids, assembles into a helical-like sheet that is stabilized by the dry hydrophobic interfaces of Phe residues. This architecture resembles that of the functional PSMα3 amyloid, highlighting the role of dry helical interfaces as a core structural motif in amyloids. Proline replacement by hydroxyproline, a major constituent of collagen, generates minimal helical-like assemblies with enhanced mechanical rigidity. These results establish a framework for designing functional biomaterials based on ultrashort helical protein elements.

Figures
Products