One of the major research interests of our group is to design peptides for intracellular delivery based on the understanding of the molecularinterplay between peptides and membranes. Thus, the spider toxin-derived peptide, L17E, was developed and was found capable of delivering biomacromolecules into cells. This peptide was obtained by substituting a hydrophobic leucine (Leu) to a negatively charged glutamic acid (Glu) to reduce hydrophobic interactions, thereby attenuating the membrane lytic activity on cell surfaces. In the presence of L17E, the efficient intracellular delivery of a ribosome-inactivation protein (saporin), Cre recombinase and antibody (IgG) was accomplished, resulting in specificlabeling of the cytosolic proteins and subsequent suppression of the glucocorticoid receptor-mediated transcription. Another example of a redesignedlytic peptide is the venom peptide MastoparanX bearing a tri-glutamate unit and a Ni(II)-dipicolylamineat the N-terminus. Using this peptide, various fluorescently labeled macromolecules were successfully delivered to the cytosol, enabling live-cell imaging of acetylated histones.

Redesigning cationic lytic peptides to promote the delivery of biomacromolecules into cell interiors

2019 Fall National Meeting

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