Electrostatic control of thickness and stiffness in a designed protein fiber

Papapostolou, D; Bromley, EHC; Bano, C; Woolfson, DN

Abstract

Attempts to design peptide-based fibers from first principles test our understanding of protein folding and assembly, and potentially provide routes to new biomaterials. Several groups have presented such designs based on a-helical and beta-strand building blocks. A key issue is this area now is engineering and controlling fiber morphology and related properties. Previously, we have reported the design and characterization of a self-assembling peptide fiber (SAF) system based on a-helical coiled-coil building blocks. With preceding designs, the SAFs are thickened, highly ordered structures in which many coiled coils are tightly bundled. As a result, the fibers behave as rigid rods. Here we report successful attempts to design new fibers that are thinner and more flexible by further programming at the amino-acid sequence level. This was done by introducing extended, or "smeared", electrostatic networks of arginine and glutamate residues to the surfaces of the coiled-coil building blocks. Furthermore, using arginine-rather than lysine-in these networks plays a major role in the fiber assembly, presumably by facilitating multidentate intra and intercoiled-coil salt bridges.

Citation

Papapostolou, D., Bromley, E., Bano, C., & Woolfson, D. (2008). Electrostatic control of thickness and stiffness in a designed protein fiber. Journal of the American Chemical Society, 130(15), 5124-5130. https://doi.org/10.1021/ja0778444

• Journal Article Type: Article
• Publication Date: 2008
• Journal: Journal of the American Chemical Society
• Print ISSN: 0002-7863
• Electronic ISSN: 1520-5126
• Publisher: American Chemical Society
• Volume: 130
• Issue: 15
• Pages: 5124-5130
• DOI: https://doi.org/10.1021/ja0778444
• Public URL: https://durham-repository.worktribe.com/output/1546246