TY - JOUR
T1 - A multifunctional surfactant catalyst inspired by hydrolases
AU - Nothling, Mitchell D.
AU - Xiao, Zeyun
AU - Hill, Nicholas S.
AU - Blyth, Mitchell T.
AU - Bhaskaran, Ayana
AU - Sani, Marc Antoine
AU - Espinosa-Gomez, Andrea
AU - Ngov, Kevin
AU - White, Jonathan
AU - Buscher, Tim
AU - Separovic, Frances
AU - O’Mara, Megan L.
AU - Coote, Michelle L.
AU - Connal, Luke A.
PY - 2020/4/1
Y1 - 2020/4/1
N2 - 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.
AB - 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.
KW - Surfactant
KW - Catalyst
KW - Hydrolases
UR - http://www.scopus.com/inward/record.url?scp=85083071317&partnerID=8YFLogxK
UR - http://purl.org/au-research/grants/ARC/DP200100535
U2 - 10.1126/sciadv.aaz0404
DO - 10.1126/sciadv.aaz0404
M3 - Article
C2 - 32270041
AN - SCOPUS:85083071317
VL - 6
JO - Science Advances
JF - Science Advances
SN - 2375-2548
IS - 14
M1 - eaaz0404
ER -