Claudia Boccardi

TL;DR: It is shown that this chimeric peptide effectively increases cargo-molecule cytoplasm availability and allows the subsequent intracellular localization of diverse membrane-impermeable molecules (i.e. Tat(11)-EGFP fusion protein, calcein, dextrans, and plasmidic DNA) with no detectable cytotoxicity.

TL;DR: The possibility to design novel AMP sequences with non-natural amino acids was achieved through a flexible computational approach, based on chemophysical profiles of peptide sequences, via Quantitative structure-activity relationship (QSAR) descriptors.

TL;DR: FRET between suitably-labeled peptide and DNA modules was exploited to monitor complex disassembly during endocytosis, and this process is correlated to transfection timing and efficiency, which can open the way to the rational design and application of CM18-Tat11–based systems for gene-delivery purposes.

TL;DR: It is demonstrated that membrane crossing can occur with apolar payloads while it is completely inhibited by polar ones, and that peptide self-aggregation is a necessary –yet not sufficient– step for effective membrane translocation.

TL;DR: Data support a model in which NPs induce membrane perturbation in the form of transient pores on all cellular membranes, while the peptide stabilizes membrane defects selectively within endosomes, and argues that this result represents a paradigmatic example that can open the way to other targeted delivery protocols.