Noncovalently cross-linked networks are attractive hydrogel platforms because of their facile fabrication, dynamic behavior, and biocompatibility. The majority of noncovalently cross-linked hydrogels, however, exhibits poor mechanical properties, which significantly limit their utility in load bearing applications. To address this limitation, hydrogels are presented composed of micelles created from genetically engineered, amphiphilic, elastin-like polypeptides that contain a relatively large hydrophobic block and a hydrophilic terminus that can be cross-linked through metal ion coordination. To create the hydrogels, heat is firstly used to trigger the self-assembly of the polypeptides into monodisperse micelles that display transition metal coordination motifs on their coronae, and subsequently cross-link the micelles by adding zinc ions. These hydrogels exhibit hierarchical structure, are stable over a large temperature range, and exhibit tunable stiffness, self-healing, and fatigue resistance. Gels with polypeptide concentration of 10%, w/v, and higher show storage moduli of ≈1 MPa from frequency sweep tests and exhibit self-healing within minutes. These reversibly cross-linked, hierarchical hydrogels with enhanced mechanical properties have potential utility in a variety of biomedical applications.

Surfaces modified with thermoresponsive poly(N-isopropylacrylamide) (PNIPAAm) support mild and efficient harvesting of anchorage-dependent cells. To enable cellular detachment, however, the surfaces must exhibit a narrow range of PNIPAAm thicknesses. In this work, this limitation is circumvented by introducing nanopatterns to grafted PNIPAAm brushes, eliminating the critical thickness requirement for cell-culturing applications. Nanopatterned PNIPAAm surfaces are prepared using a combination of interferometric lithography (IL) and surface-initiated polymerization. Above the lower critical solution temperature (LCST) of PNIPAAm (∼32 °C), these surfaces support the attachment and proliferation of mammalian cells (e.g., fibroblasts and endothelial cells). Below the LCST of PNIPAAm, cells readily detach from the nanopatterned PNIPAAm surfaces without influence from the period of nanopatterns, which vary between 157 ± 9 nm to 1021 ± 17 nm. Cells selectively attach and proliferate on PNIPAAm nanopatterns as compared to thick unpatterned PNIPAAm, which is further exploited to spatially direct cellular growth to generate cellular micropatterns. Nanopatterned PNIPAAm surfaces provide a unique solution to the critical thickness issue for cell harvesting and facilitate spatial control of cellular growth on surfaces.

Infectious biofilms are problematic in many healthcare-related devices and are especially challenging and ubiquitous in urinary catheters. This report presents an on-demand fouling-release methodology to mechanically disrupt and remove biofilms, and proposes this method for the active removal of infectious biofilms from the previously inaccessible main drainage lumen of urinary catheters. Mature Proteus mirabilis crystalline biofilms detach from silicone elastomer substrates upon application of strain to the substrate, and increasing the strain rate increases biofilm detachment. The study presents a quantitative relationship between applied strain rate and biofilm debonding through an analysis of biofilm segment length and the driving force for debonding. Based on this mechanism, hydraulic and pneumatic elastomer actuation is used to achieve surface strain selectively within the lumen of prototypes of sections of a fouling-release urinary catheter. Proof-of-concept prototypes of sections of active, fouling-release catheters are constructed using techniques typical to soft robotics including 3D printing and replica molding, and those prototypes demonstrate release of mature P. mirabilis crystalline biofilms (e.g., ≈90%) from strained surfaces. These results provide a basis for the development of a new urinary catheter technology in which infectious biofilms are effectively managed through new methods that are entirely complementary to existing approaches.

Nucleation and growth methods offer scalable means of synthesizing colloidal particles with precisely specified size for applications in chemical research, industry, and medicine. These methods have been used to prepare a class of silicone gel particles that display a range of programmable properties and narrow size distributions. The acoustic contrast factor of these particles in water is estimated and can be tuned such that the particles undergo acoustophoresis to either the pressure nodes or antinodes of acoustic standing waves. These particles can be synthesized to display surface functional groups that can be covalently modified for a range of bioanalytical and acoustophoretic sorting applications.

Nucleation and growth methods offer scalable means of synthesizing colloidal particles with precisely specified size for applications in chemical research, industry, and medicine. These methods have been used to prepare a class of silicone gel particles that display a range of programmable properties and narrow size distributions. The acoustic contrast factor of these particles in water is estimated and can be tuned such that the particles undergo acoustophoresis to either the pressure nodes or antinodes of acoustic standing waves. These particles can be synthesized to display surface functional groups that can be covalently modified for a range of bioanalytical and acoustophoretic sorting applications.

Elastin-like polypeptide (ELP) fusions have been designed to allow large-scale, nonchromatographic purification of many soluble proteins by using the inverse transition cycling (ITC) method; however, the sensitivity of the aqueous lower critical solubility phase transition temperature (T_t) of ELPs to the addition of cosolutes, including detergents, may be a potential hindrance in purification of proteins with surface hydrophobicity in such a manner. To identify detergents that are known to solubilize such proteins (e.g., membrane proteins) and that have little effect on the T_t of the ELP, we screened a number of detergents with respect to their effects on the T_t and secondary structures of a model ELP (denoted here as ELP180). We found that mild detergents (e.g., n-dodecyl-β-D-maltoside, Triton-X100, and 3-[(3-cholamidopropyl) dimethylamino]-1-propanesulfonate) do not alter the phase transition behavior or structure (as probed by circular dichroism) of ELP180. This result is in contrast to previous studies that showed a strong effect of other detergents (e.g., sodium dodecylsulfate) on the T_t of ELPs. Our results clearly indicate that mild detergents do not preclude ITC-based separation of ELPs, and thus that ELP fusions may prove to be useful in the purification of detergent-solubilized recombinant hydrophobic proteins, including membrane proteins, which are otherwise notoriously difficult to extract and purify by conventional separation methods (e.g., chromatography). © 2012 Wiley Periodicals, Inc.