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.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.