An Efficient Electrochromic Supercapacitor Based on Solution-Processable Nanoporous Poly{tris[4-(3,4-ethylenedioxythiophene)phenyl]amine}.

A new green synthetic route to tris[4-(3,4-ethylenedioxythiophene)phenyl]amine (TEPA) monomer has been developed and the molecular structure of TEPA has been determined by using single-crystal XRD. Solution-processable nanoporous poly{tris[4-(3,4-ethylenedioxythiophene)phenyl]amine} (PTEPA) is prepared by a chemical oxidative polymerization in a microemulsion. Based on the distorted structure of TEPA in the solid state, it is proposed that dendritic PTEPA has a distorted 3 D conformation with multiple twisted channels and pores that are narrowed and blocked by bifurcation and distortion of PTEPA, which is consistent with the observed hierarchical pore structure. As a cathode material, PTEPA exhibits a discharge capacity of 89.5 mAh g-1 in the initial cycle with a highly sloping two-stage discharge curve and relatively stable cycling performance. Beyond its excellent energy storage properties, PTEPA also shows relatively good electrochromic performance. Furthermore, an efficient all-solid-state electrochromic supercapacitor (ECSC) with good electrochromic performance and high energy storage capacity (13.3 mF cm-2 ) is assembled from PTEPA and nanoporous graphene films. During charge-discharge processes, the color of the ECSC changes between yellow-green and steel blue. Thus, the energy storage level of the ECSC can be monitored by the corresponding color changes. The fabricated ECSC may have practical applications, for example, in self-powered electrochromic smart windows.

Neutralizing antibodies of botulinum neurotoxin serotype A screened from a fully synthetic human antibody phage display library.

The botulinum neurotoxins (BoNTs) produced by Clostridium botulinum are the most poisonous protein substances known. The neutralizing antibodies against botulinum neurotoxin can effectively prevent and cure the toxicosis. Using purified Hc fragments of botulinum neurotoxin serotype A (BoNT/A-Hc) as antigen, 2 specific neutralizing antibodies mapping different epitopes were selected from a fully synthetic human antibody library. The 2 antibodies can effectively inhibit the binding between BoNT/A-Hc and differentiated PC-12 cells in vitro, and the neutralization was evaluated in vivo. Although no single mAb completely protected mice from toxin, they both could prolong time to death when challenged with 20 LD(50)s (50% lethal doses) of BoNT/A. When used together, the mAbs completely neutralized 1000 LD(50)s/mg Ab, suggesting their high neutralizing potency in vivo. The results would lead to further production of neutralizing antibody drugs against BoNT/A. It also proved that it was a quick method to obtain human therapeutic antibodies by selecting from the fully synthetic human antibody phage display library.

[Eukaryotic expression of P-selectin functional segment on the membrane of CHO].

Cell adhesive molecular P-selectin was cloned, expressed and anchored on CHO cell membrane through GPI for selection specific antibodies. Total human platelet RNA was extracted and the functional segment of P-selectin gene was cloned by RT-PCR. The P-selectin functional segment gene was cloned into a eukaryotic expression vector pMCEw2-GPI containing an attenuated neo gene together with a downstream GPI, which was synthesized by overlapping PCR. The recombinant plasmid pMCEw2-GPI-P-selectin was then transfected to CHO(dhfr-) cells and screened with G418. ELISA, western-blot and immunofluorescence were carried out to detect the stability of P-selection expression on cell membrane. These results provided a necessary basis for the following study of selection the antibodies targeting P-selectin.