Nanomechanics of Streptavidin Hubs for Molecular Materials
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.
Keywords: protein-based materials ; molecular self-assembly ; single molecule force spectroscopy ; scanning probe microscopy ; polypeptides ; biomaterials ; Atomic-Force Microscopy ; Protein-Ligand Interaction ; Tag Ii Peptide ; Biotin-Binding ; Mechanical-Properties ; Core Streptavidin ; Biomaterials ; Stability ; Affinity ; Muscle
Record created on 2012-06-12, modified on 2016-08-09