Cell-penetrating peptides (CPP) transport molecular cargo into cells via membrane translocation. HipC, the C-terminal domain of the antimicrobial peptide Hipposin, is able to translocate into E. coli cells without causing significant membrane lysis. This study investigates the ability of HipC to confer cell-penetrating properties to other peptides by combing it with a membrane inactive TM1 domain from the mechanosensitive channel of large conductance (MscL). This characterization was considered by the antimicrobial activity of these chimeric proteins in addition to their translocation ability into large unilamellar vesicles. The secondary structure of the two constructs can also be considered via circular dichroism, allowing a comparison of how cell-penetrating and antimicrobial mechanisms relate to protein conformation. Understanding how the non-lytic, membrane translocating HipC can transfer cargo into a cell can better influence the design of CPPs with specific functions, including drug delivery and further research applications.

Cell-penetrating characterization of antimicrobial peptide hipposin

247th National Meeting (2014)

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