The remarkable power of enzymes to undertake catalysis frequently stems from their grouping of multiple, complementary chemical units within close proximity around the enzyme active site. Motivated by this, we report here a bioinspired surfactant catalyst that incorporates a variety of chemical functionalities common to hydrolytic enzymes. The textbook hydrolase active site, the catalytic triad, is modeled by positioning the three groups of the triad (-OH, -imidazole, and -CO₂H) on a single, trifunctional surfactant molecule. To support this, we recreate the hydrogen bond donating arrangement of the oxyanion hole by imparting surfactant functionality to a guanidinium headgroup. Self-assembly of these amphiphiles in solution drives the collection of functional headgroups into close proximity around a hydrophobic nano-environment, affording hydrolysis of a model ester at rates that challenge α-chymotrypsin. Structural assessment via NMR and XRD, paired with MD simulation and QM calculation, reveals marked similarities of the co-micelle catalyst to native enzymes.

酶进行催化作用的强大能力通常源于它们在酶活性位点附近的多个互补化学单元的分组。因此，我们在此报告了一种受生物启发的表面活性剂催化剂，该催化剂结合了水解酶常见的多种化学功能。教科书的水解酶活性位点，催化三联体，是通过定位三联体的三个基团（-OH，-咪唑和-CO ₂H）在单个三官能表面活性剂分子上。为支持这一点，我们通过将表面活性剂官能团赋予胍基头基来重建氧阴离子孔的氢键供体排列。这些两亲物在溶液中的自组装驱动功能性头基的收集在疏水性纳米环境周围紧密接近，从而以挑战α-胰凝乳蛋白酶的速率提供了模型酯的水解作用。通过NMR和XRD进行的结构评估，以及MD模拟和QM计算相结合，揭示了胶束催化剂与天然酶的显着相似性。