Tecnai g2 f20 u twin

The morphologies of the PINPs and PINPs@PM were obtained by TEM (Tecnai G2 F20 U-TWIN, FEI, Hillsboro, OR, US). To confirm the PM camouflage, PINPs@PM was denatured and resolved via 10% SDS-PAGE. The protein bands were visualized by Coomassie blue staining. The DLS and zeta potential experiments were determined by a Nano-ZS (Malvern, Worcestershire, UK) at room temperature. The temperature alteration of PINPs@PM exposed to NIR at 808 nm for different times (1.0 W/cm², Laserwave, Beijing, CHN) was recorded with a thermoelectric thermometer (HH806W, Omega, US).

As-prepared chiral polyaniline (0.1 mL) was first diluted in 1.8 mL of good solvent in a test tube in the presence of a uniaxial stretched polypropylene (PP) template. Then, 2.2 mL of poor solvent methanol was added into the above solution. The mixture was vigorously shaken for 1 min and left to stand for days for self-assembly. As-prepared PANI membrane adhere to the PP template was peeled down in THF into the flat macro stripe, and the stripe transformed into a helical macroribbon in THF/iPrOH co-solvents. These macrostructures were recorded by optical microscopy (VHX-5000, Keyence). The stripe or ribbon was transferred on silicon wafer or carbon-coated copper grid for SEM (S-4800 or S-8220, Hitachi, Japan), AFM (M-Pico, Multimode Veeco), TEM and SAED (Tecnai G2 F20U-TWIN, FEI Co., USA) characterization. Dried samples transferred on copper grid and stripes immersed in the solvents of THF and iPrOH in quartz capillaries were used for WAXS characterization, respectively (Xeuss small-angle and wide-angle X-ray scattering system with Xenocs Cu Kα X-ray source GeniX Cu ULD and Dectris 100 K Pilatus). The ribbon dispersed in co-solvent with different Φ_iPrOH were characterised by CD and UV-vis-IR spectra.

Briefly, E. coli were cultured as described above, then removed by centrifugation at 5000×g for 10 min at 4 °C. The resulting supernatant (200 mL) was filtered through a 0.45-µm EPS filter (Millipore), then concentrated to 50 mL using a 50-K ultrafiltration tube. The concentrated solution was further filtered with a 0.22-µm EPS membrane (Millipore). OMVs were collected from the filtrate by ultracentrifugation at 150,000×g for 3 h at 4 °C. The collected OMVs were washed with PBS using centrifugation at 150,000×g for 2 h at 4 °C, then finally resuspended in 400 μL PBS and stored at −20 °C until use. The total protein concentration of OMVs preparations was evaluated using the bicinchoninic acid assay, the results of which were defined as the OMVs WT concentration. The size and morphology of the OMVs were characterized using dynamic light scattering (DLS) (Zetasizer Nano ZS90, Malvern, UK) and transmission electron microscopy (TEM) (Tecnai G2 F20 U-TWIN, FEI, USA). The LPS content in OMV was detected by ELISA (CEB526Ge, Cloud-Clone Corp., Wuhan, China) and LAL assay (L00350C, GenScript, Nanjing, China).

The microstructure and morphology of the as-prepared sponges were characterized by SEM (HITACHI S3400). To give an insight of inter-tube structure, TEM (FEI Tecnai G2 F20 U-TWIN) observations were conducted directly on as-prepared samples. Thin CNT sheets were carefully separated from the CNT materials and directly deposited between two TEM grids to observe their initial inter-tube structure. For the electromechanical tests, the top and bottom surfaces of the CNT sponges were coated with a uniform layer of silver paste and connected by silver wires. During the compression process, the electrical resistance (Keithley 4200 SCS under a bias of 10 mA) was recorded simultaneously.