Protein
Binding-Induced Surfactant Aggregation Variation:
A New Strategy of Developing Fluorescent Aqueous Sensor for Proteins
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Abstract
Novel strategies of developing fluorescent
sensors for proteins
are highly demanded. In this work, we particularly synthesized a cholesterol-derivatized
pyrene probe. Its fluorescence emission is effectively tuned by the
aggregation state of a cationic surfactant dodecyltrimethylammonium
bromide (DTAB). The used probe/DTAB assemblies exhibit highly sensitive
ratiometric responses to pepsin and ovalbumin egg (o-egg) with detection
limits of 4.8 and 18.9 nM, respectively. The fluorescence changes
indicate the protein–surfactant interaction leads to further
aggregation of DTAB assemblies. The results from Tyndall effect and
dynamic light scattering verify this assumption. The responses to
pepsin and o-egg are due to their strong electrostatic or hydrophobic
interaction with DTAB assemblies at pH 7.4. The present noncovalent
supramolecular sensor represents a novel and simple strategy for sensing
proteins, which is based on the encapsulated fluorophore probing the
aggregation variation of the surfactant assemblies