A multifunctional surfactant catalyst inspired by hydrolases

Mitchell D. Nothling, Zeyun Xiao, Nicholas S. Hill, Mitchell T. Blyth, Ayana Bhaskaran, Marc Antoine Sani, Andrea Espinosa-Gomez, Kevin Ngov, Jonathan White, Tim Buscher, Frances Separovic, Megan L. O’Mara, Michelle L. Coote, Luke A. Connal*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    46 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Article numbereaaz0404
    JournalScience advances
    Volume6
    Issue number14
    DOIs
    Publication statusPublished - 1 Apr 2020

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