Split intein-mediated backbone cyclization enhances the stability and activity of staphylokinase, a potent fibrin-selective plasminogen activator

细菌的 plasminogen 使活跃之物 staphylokinase (Sak ) 是为对待尖锐心肌的梗塞的一个有希望的 thrombolytic 代理人。为了有效地减少 Sak 的 immunogenicity，当维持它的 fibrinolytic 活动时，地点特定的 PEGylation 在现在的学习被执行。chemoselective 半胱氨酸 PEGylation 地点在一个 immunodominant 区域以内被选择(氨基酸残余 7187 ) 用一在里面 silico 途径。在这研究准备的 PEGylated Sak 变体显示出纯净 >97.0% 。在位置 80 点的 PEGylation 导致了与本国的 recombinant staphylokinase (r-Sak ) 相比举办类似的 fibrinolytic 活动和 thermostability 的 Sak 变体 Sak (E80C 木钉) 。在畿尼猪的 Sak (E80C 木钉) 的 immunogenicity 极大地与本国的 r-Sak 相比被减少。而且，初步的 pharmacokinetic 结果建议来自兔子的血溪流的 Sak (E80C 木钉) 的血浆清理显著地与 r-Sak 的相比被减少，导致起始的半衰期的 2.8 褶层增加和全身的可获得性的 3.8 褶层增加。在摘要，这些结果证明地点特定的 PEGylation 与超越未修改的 Sak 的显著优点产出新奇 Sak 变体 Sak (E80C 木钉) 。

Effect of site-specific PEGylation on the fibrinolytic activity, immunogenicity, and pharmacokinetics of staphylokinase

The elimination of residual host cell DNA (HCD) and proteins (HCPs) is a pivotal step in the purification process for biological products such as monoclonal antibodies, recombinant proteins, vaccines, gene therapy vectors, and cell‐based therapies. During the preparation of recombinant staphylokinase (r‐SAK), a potential therapeutic protein for thrombotic disorders expressed in Escherichia coli cells, an efficient chromatography purification process, incorporating anion exchange, cation exchange, and gel filtration techniques, was developed to effectively eliminate HCPs and residual DNA. This multistep chromatography approach yielded r‐SAK with a residual HCD concentration below 1 ng/mL, a residual HCP concentration below 0.01%, and purity exceeding 98%. Comparative analysis revealed that modified cellulose‐based matrix resins exhibited superior efficiency compared to dextran and agarose matrix resins for eliminating residual HCPs and HCD under identical conditions. Based on the different properties of the matrix, deductions were made regarding the reasons for the differentiation in separation efficiency. The physical strength of the cellulose‐based matrix ensures the structural stability of macroporous resin and can guarantee efficient separation under conditions of high flow and heavy load. This study suggests that maintaining the structural stability of macropores in bioseparation materials is crucial for improving the efficiency of separating biological products.

Removal of Residual DNA and Host Cell Proteins for the Purification of Recombinant Staphylokinase Expressed in Escherichia coli

Purification and in vivo stability and half-life of recombinant lipid modified staphylokinase.

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Purification and in vivo stability and half-life of recombinant lipid modified staphylokinase.