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To exploit efficient adsorbents for removing middle molecular peptides containing DFLAE (DE5,a typical peptide sequence accumulated in uremic serum) sequence by hemoperfusion,we designed and synthesized three affinity adsorbents (C1-Zn2+,C2-Zn2+ and C3-Zn2+) that could have high affinity to DE5.Subsequently,we evaluated the corresponding adsorption ability of each adsorbent by static adsorption experiments and isothermal titration calorimetry (ITC).The results showed that C1-Zn2+ had the best adsorption ability to DE5-containing peptides and the adsorption capacity for DE5 was 8.52 mg/g.By changing the adsorption conditions,the adsorption mechanism was elucidated.The main driving force of the adsorption is metal-carboxyl coordination and the hydrophobic force affords the cooperative effect.It is expected that our present work can provide basic understanding for the design of adsorbents with high affinity and selectivity towards oligopeptides.
To exploit efficient adsorbents for removing middle molecular peptides containing DFLAE (DE5, a typical peptide sequence accumulated in uremic serum) sequence by hemoperfusion, we designed and synthesized three affinity adsorbents (C1-Zn2 +, C2-Zn2 + and C3-Zn2 +) that could have high affinity to DE5.Subsequently, we evaluated the corresponding adsorption ability of each adsorbent by static adsorption experiments and isothermal titration calorimetry (ITC). The results showed that C1-Zn2 + had the best adsorption ability to DE5-containing peptides and the adsorption capacity for DE5 was 8.52 mg / g.By changing the adsorption conditions, the adsorption mechanism was elucidated. The main driving force of the adsorption is metal-carboxyl coordination and the hydrophobic force affords the cooperative effect. It is expected that that present work work can provide basic understanding for the design of adsorbents with high affinity and selectivity towards oligopeptides.