Rheology of binary colloidal structures assembled via specific biological cross-linking.
The selectivity and range of energies offered by specific biological interactions serve as valuable tools for engineering the assembly of colloidal particles into novel materials. In this investigation, high affinity biological interactions between biotin-coated "A" particles (RA = 0.475 microm) and streptavidin-coated "B" particles (RB = 2.75 microm) drive the self-assembly of a series of binary colloidal structures, from colloidal micelles (a large B particle coated by smaller A particles) to elongated chain microstructures (alternating A and B particles), as the relative number of small (A) to large (B) particles (2 < or = NA/NB < or = 200) is decreased at a low total volume fraction (10(-4) < or = phiT < or = 10(-3)). At a significantly higher total volume fraction (phiT > or = 10(-1)) and a low number ratio (NA/NB = 2), the rheological behavior of volume-filling particle networks connected by streptavidin-biotin bonds is characterized. The apparent viscosity (eta) as a function of the shear rate gamma, measured for networks at phiT = 0.1 and 0.2, exhibits shear-rate-dependent flow behavior, and both the apparent viscosity and the extent of shear thinning increase upon an increase of a factor of 2 in the total volume fraction. Micrographs taken before and after shearing show a structural breakdown of the flocculated binary particle network into smaller flocs, and ultimately a fluidlike suspension, with increasing shear rate. Rheological measurements provide further proof that suspension microstructure is governed by specific biomolecular interactions, as control experiments in which the streptavidin molecules on particles were blocked displayed Newtonian flow behavior. This investigation represents the first attempt at measuring the rheology of colloidal suspensions where assembly is driven by biomolecular cross-linking.
Department of Chemical and Biomolecular Engineering and Laboratory for Research on the Structure of Matter, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Amy L
AL
Hiddessen
David A
DA
Weitz
Daniel A
DA
Hammer
D001710:Biotin / Q000737:chemistry*; D003102:Colloids / Q000737:chemistry*; D008823:Micelles; D010316:Particle Size; D012212:Rheology / Q000379:methods; D019809:Streptavidin / Q000737:chemistry*; D013499:Surface Properties
D003102:Colloids; D008823:Micelles; D001710:Biotin; D019809:Streptavidin