In order to improve the functional affinity of the humanized VH single domain antibody against human lung cancer, the genes coding the homogenous dimers dihu3D3Vn and tetramers tehu3D3VH were constructed by fusing the...In order to improve the functional affinity of the humanized VH single domain antibody against human lung cancer, the genes coding the homogenous dimers dihu3D3Vn and tetramers tehu3D3VH were constructed by fusing the SV5-Cys short peptide and p53 tetramefization structural domain gene to hu3D3VH gene via recombinant PCR technique, respectively. Then, the dihu3D3VH and tehu3D3VH genes were cloned to the prokaryotic expression vector pET-22b（ ＋ ） and expressed in E. coli BL21 （DE3）. The proteins expressed were purified through Ni^2＋ -affinity chromatographic column. Meanwhile, the hu3D3VH, dihu3D3VH and tehu3D3VH proteins were labeled with FTTC, and their reactivity with antigen and specificity were analyzed by immunofluorescence assay. As to their functional affinities, it was analyzed and compared by flow cytometry. The results indicated that these two genes were expressed as monomers and mainly as inclusion bodies. After purification and renaturation, there were about 50% of dimers and 70% of tetramer remaining in the protein solution. In addition, the dihu3D3VH and tehu3D3VH proteins still remained the reactivity with antigen and specificity of hu3D3VH protein, and their functional affinities were increased about 60% or 100% respectively, compared with those of hu3D3VH protein. It is evident that the functional affinity of hu3D3VH protein can be greatly improved by increasing its binding valency.展开更多
The development of aqueous zinc-ion batteries (AZIBs) marks a significant advancement in the field of sustainable and environmentally friendly energy storage.To address the challenges faced by singlephase vanadium-bas...The development of aqueous zinc-ion batteries (AZIBs) marks a significant advancement in the field of sustainable and environmentally friendly energy storage.To address the challenges faced by singlephase vanadium-based oxides,such as poor conductivity and dissolution in electrolytes,this study introduces vacuum S/N doping to fabricate V_(2)O_(3)/VO_(2)@S/N-C nanofibers,improving the cycling stability and enhancing the capacity.The V_(2)O_(3)/VO_(2)@S/N-C electrode exhibits exceptional cyclic stability,retaining a capacity of 133.3 m A h g^(-1)after 30,000 cycles at a high current density of 100 A g^(-1)and a capacity retention of 81.8%after 150,000 cycles at 200 A g^(-1).Characterizations using ex-situ X-ray diffraction and ex-situ X-ray photoelectron spectroscopy reveal co-intercalation of H^(+)and Zn^(2+)in the V_(2)O_(3)/VO_(2)@S/N-C electrode.Due to the presence of S_(2)^(2-),more phases changed to V_(10)O_(24).12H_(2)O,making the V_(2)O_(3)/VO_(2)@S/N-C electrode better reversible.By elucidating the zinc storage mechanism and demonstrating the stable performance of the doped electrode,this work contributes valuable insights into the optimization of the electrode materials for future energy storage solutions.展开更多
文摘In order to improve the functional affinity of the humanized VH single domain antibody against human lung cancer, the genes coding the homogenous dimers dihu3D3Vn and tetramers tehu3D3VH were constructed by fusing the SV5-Cys short peptide and p53 tetramefization structural domain gene to hu3D3VH gene via recombinant PCR technique, respectively. Then, the dihu3D3VH and tehu3D3VH genes were cloned to the prokaryotic expression vector pET-22b（ ＋ ） and expressed in E. coli BL21 （DE3）. The proteins expressed were purified through Ni^2＋ -affinity chromatographic column. Meanwhile, the hu3D3VH, dihu3D3VH and tehu3D3VH proteins were labeled with FTTC, and their reactivity with antigen and specificity were analyzed by immunofluorescence assay. As to their functional affinities, it was analyzed and compared by flow cytometry. The results indicated that these two genes were expressed as monomers and mainly as inclusion bodies. After purification and renaturation, there were about 50% of dimers and 70% of tetramer remaining in the protein solution. In addition, the dihu3D3VH and tehu3D3VH proteins still remained the reactivity with antigen and specificity of hu3D3VH protein, and their functional affinities were increased about 60% or 100% respectively, compared with those of hu3D3VH protein. It is evident that the functional affinity of hu3D3VH protein can be greatly improved by increasing its binding valency.
基金financially supported by the Natural Science Foundation of China (Grant No. 52272063)the Jiangxi Provincial Natural Science Foundation (No. 20224BAB214037, 20232BAB204022, 20232BAB204019)。
文摘The development of aqueous zinc-ion batteries (AZIBs) marks a significant advancement in the field of sustainable and environmentally friendly energy storage.To address the challenges faced by singlephase vanadium-based oxides,such as poor conductivity and dissolution in electrolytes,this study introduces vacuum S/N doping to fabricate V_(2)O_(3)/VO_(2)@S/N-C nanofibers,improving the cycling stability and enhancing the capacity.The V_(2)O_(3)/VO_(2)@S/N-C electrode exhibits exceptional cyclic stability,retaining a capacity of 133.3 m A h g^(-1)after 30,000 cycles at a high current density of 100 A g^(-1)and a capacity retention of 81.8%after 150,000 cycles at 200 A g^(-1).Characterizations using ex-situ X-ray diffraction and ex-situ X-ray photoelectron spectroscopy reveal co-intercalation of H^(+)and Zn^(2+)in the V_(2)O_(3)/VO_(2)@S/N-C electrode.Due to the presence of S_(2)^(2-),more phases changed to V_(10)O_(24).12H_(2)O,making the V_(2)O_(3)/VO_(2)@S/N-C electrode better reversible.By elucidating the zinc storage mechanism and demonstrating the stable performance of the doped electrode,this work contributes valuable insights into the optimization of the electrode materials for future energy storage solutions.
