Lipases,
as well as other enzymes, are present and active within
the sea surface microlayer (SSML). Upon bubble bursting, lipases partition
into sea spray aerosol (SSA) along with surface-active molecules such
as lipids. Lipases are likely to be embedded in the lipid monolayer
at the SSA surface and thus have the potential to influence SSA interfacial
structure and chemistry. Elucidating the structure of the lipid monolayer
at SSA interfaces and how this structure is altered upon interaction
with a protein system like lipase is of interest, given the importance
of how aerosols interact with sunlight, influence cloud formation,
and provide surfaces for chemical reactions. Herein, we report an
integrated experimental and computational study of Burkholderia cepacia lipase (BCL) embedded in a lipid
monolayer and highlight the important role of electrostatic, rather
than hydrophobic, interactions as a driver for monolayer stability.
Specifically, we combine Langmuir film experiments and molecular dynamics
(MD) simulations to examine the detailed interactions between the
zwitterionic dipalmitoylphosphatidylcholine (DPPC) monolayer and BCL.
Upon insertion of BCL from the underlying subphase into the lipid
monolayer, it is shown that BCL permeates and largely disorders the
monolayer while strongly interacting with zwitterionic DPPC molecules,
as experimentally observed by Langmuir adsorption curves and infrared
reflectance absorbance spectroscopy. Explicitly solvated, all-atom
MD is then used to provide insights into inter- and intramolecular
interactions that drive these observations, with specific attention
to the formation of salt bridges or ionic-bonding interactions. We
show that after insertion into the DPPC monolayer, lipase is maintained
at high surface pressures and in large BCL concentrations by forming
a salt-bridge-stabilized lipase–DPPC complex. In comparison,
when embedded in an anionic monolayer at low surface pressures, BCL
preferentially forms intramolecular salt bridges, reducing its total
favorable interactions with the surfactant and partitioning out of
the monolayer shortly after injection. Overall, this study shows that
the structure and dynamics of lipase-embedded SSA surfaces vary based
on surface charge and pressure and that these variations have the
potential to differentially modulate the properties of marine aerosols.