The development of stimuli-responsive biomimetic systems
to understand
interactions between proteins and surfaces is of an increasingly important
scientific interest due to its potential applications in diagnostics
and fundamental biological research. In this study, we report a simple
and label-free method utilizing interfacial properties of liquid crystals
(LCs), mediated by self-assembly of a naturally occurring cyclic lipopeptide,
surfactin (SFN). We demonstrated that SFN molecules promote the homeotropic
alignment of LC at the LC–aqueous interface giving rise to
dark optical appearances under cross polars. The ordering transition
of LC is mainly caused by the lateral hydrophobic interactions between
hydrocarbon chains of SFN and LC molecules at the interface. Interestingly,
the optical state of LC changed to bright when protein (five proteins
studied herein) molecules were in the vicinity of the interface thereby,
allowing label-free imaging of protein adsorption at those interfaces.
It was further realized that the shapes of bright spatial patterns
at the SFN-laden interface, which are formed in the presence of proteins,
are directly associated with the native secondary conformations of
proteins, i.e., elongated/fibrillar (β-sheet-rich) and globular
domains (α-helix-rich). Thus, the designed LC system can also
be applied to detect amyloidogenic proteins, mainly involved in neurological
disorders. In addition, the LC-based method presents additional advantages
over existing spectroscopic/biological techniques such as simple optical
readout, high sensitivity (nanomolar concentration regime), and easy
sample preparation. We believe that the SFN-decorated LC-based interfaces
will open a new avenue to detect other subtle biomolecular interactions
at LC–aqueous interfaces.