title: Nanomechanics of streptavidin hubs for molecular materials.
abstract: A new strategy is reported for creating protein-based nanomaterials by genetically fusing large polypeptides to monomeric streptavidin and exploiting the propensity of streptavidin monomers(SM) to self-assemble into stable tetramers. We have characterized the mechanical properties of streptavidin-linked structures and measured, for the first time, the mechanical strength of streptavidin tetramers themselves. Using streptavidin tetramers as molecular hubs offers a unique opportunity to create a variety of well-defined, self-assembled protein-based (nano)materials with unusual mechanical properties.
authors.affiliation: Department of Mechanical Engineering and Materials Science, Center for Biologically Inspired Materials and Material Systems, Duke University, Durham, NC 27708, USA.
authors.forename: Minkyu
authors.initials: M
authors.lastname: Kim
authors.forename: Chien-Chung
authors.initials: CC
authors.lastname: Wang
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Benedetti
authors.forename: Mahir
authors.initials: M
authors.lastname: Rabbi
authors.forename: Vann
authors.initials: V
authors.lastname: Bennett
authors.forename: Piotr E
authors.initials: PE
authors.lastname: Marszalek
mesh_terms: D001672:Biocompatible Materials / Q000737:chemistry*; D001696:Biomechanical Phenomena; D018625:Microscopy, Atomic Force; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure; D010455:Peptides / Q000737:chemistry; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D055550:Protein Stability; D019809:Streptavidin / Q000737:chemistry*; D013499:Surface Properties; D013696:Temperature
chemical_list: D001672:Biocompatible Materials; D010455:Peptides; D019809:Streptavidin
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