Abstract
ABSTRACTIn this work, we investigate the feasibility of using a surface-tethered heptapeptide sequence as the basis for a ferroelectric-actuated component in a nanofluidic device. The fluorescently-labeled peptide sequence, (CISLLHSTC) is shown by fluorescence microscopy to selectively coat the PZT patterned channel floors. The peptide binding strength to PZT is determined over a range of flow rates in the patterned channel by imaging the fluorescence intensity of the coated channel and monitoring the output spectroscopically. The peptide is found to be stripped from the PZT at flow rates exceeding 5mL/h. Initial results demonstrating the possibility of covalently integrating the short peptide sequence to larger biological components such as antibodies are also presented.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have