Cryo-Transmission Electron Microscopy Structure of a Gigadalton Peptide Fiber of De Novo Design
Cryo-transmission electron microscopy structure of a gigadalton peptide fiber of de novo design Thomas H. Sharpa,b, Marc Bruninga,1, Judith Mantellb,c,1, Richard B. Sessionsb,1, Andrew R. Thomsona,1, Nathan R. Zaccaib,1, R. Leo Bradyb, Paul Verkadeb,c,d,2, and Derek N. Woolfsona,b,2 aSchool of Chemistry, University of Bristol, Cantock’s Close, Bristol BS8 1TS, United Kingdom; bSchool of Biochemistry, University of Bristol, University Walk, Bristol BS8 1TD, United Kingdom; cWolfson Bioimaging Facility, University of Bristol, Bristol BS8 1TD, United Kingdom; and dSchool of Physiology and Pharmacology, University of Bristol, Bristol BS8 1TD, United Kingdom Edited by David Baker, University of Washington, Seattle, WA, and approved July 6, 2012 (received for review November 21, 2011) Nature presents various protein fibers that bridge the nanometer of α-helical coiled coils, remain relatively poorly described at to micrometer regimes. These structures provide inspiration for the the assembly, molecular, and atomic levels (7–9). de novo design of biomimetic assemblies, both to address difficul- From a more-applied perspective, interest in peptide- and pro- ties in studying and understanding natural systems, and to provide tein-based fibrous biomaterials has increased recently because routes to new biomaterials with potential applications in nano- these materials have potential applications in biotechnology and technology and medicine. We have designed a self-assembling fi- synthetic biology—for example, as scaffolds for 3D cell culture, ber system, the SAFs, in which two small α-helical peptides are tissue engineering, and templating the assembly of functional in- programmed to form a dimeric coiled coil and assemble in a con- organic materials (10–13).
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