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Cellular localisation of CPPs and transduced proteins

The localisation of CPPs and transduced cargoes in cells after internalisation has not been unambiguously defined despite of numerous studies by fluorescence techniques. We characterised the cellular whereabouts of CPPs and delivered cargo protein molecules in the cell interior by using electron (and also fluorescence) microscopy. The transport peptides concentrate on the plasma membrane and typically to microvillar or filopodial structures that seem to mediate first association. In cells interior CPPs show wide distribution, localising to endocytotic vesicles but also in cytoplasm, Golgi region and to some extent in nuclei and mitochondria.

Protein molecules coupled to transport peptide non-covalently accumulate on the cell surface before entering cells. In analogy with CPPs, the first association of delivered protein occurs often at cell-surface extensions. CPP-protein complexes are taken up by cells mostly in vesicular structures that differ by size and morphology. CPP-protein constructs at high concentration induce formation of large endosomes reminiscent macropinosomes and constructs are confined to vesicular structures mostly. At lower CPP-protein constructs concentrations small vesicles pinch off from the plasma membrane into cells and the complexes are detected in the cytoplasm and Golgi region outside vesicles.

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