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Aggregation Behavior of giant amphiphiles prepared by cofactor reconstitution

机译：辅因子重构制备的巨型两亲物的聚集行为

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摘要

We report on biohybrid surfactants, termed "giant amphiphiles", in which a protein or an enzyme acts as the polar head group and a synthetic polymer as the apolar tail. It is demonstrated that the modification of horseradish peroxidase (HRP) and myoglobin (Mb) with an apolar polymer chain through the cofactor reconstitution method yields giant. amphiphiles that form spherical aggregates (vesicles) in aqueous solution. Both HRP and Mb retain their original functionality when modified with a single polystyrene chain, but reconstitution has an effect on their activities. In the case of HRP the enzymatic activity decreases and for Mb the stability of the dioxygen myoglobin (oxy-Mb) complex is reduced, which is probably the result of a disturbed binding of the heme in the apo-protein or a reduced access of the substrate to the active site of the enzyme or protein.
机译：我们报道了称为“巨型两亲物”的生物杂交表面活性剂，其中蛋白质或酶充当极性头基团，合成聚合物充当非极性尾巴。结果表明，通过辅因子重构方法用非极性聚合物链修饰辣根过氧化物酶（HRP）和肌红蛋白（Mb）产生巨大的变化。在水溶液中形成球形聚集体（小泡）的两亲物。当用单条聚苯乙烯链修饰时，HRP和Mb都保留其原始功能，但是重组会影响其活性。在HRP的情况下，酶活性降低，而对于Mb，双氧肌红蛋白（oxy-Mb）复合物的稳定性降低，这很可能是血红素在脱辅基蛋白中的结合受阻或血红蛋白通路减少的结果。酶或蛋白质活性位点的底物。

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