title: Protein transduction: unrestricted delivery into all cells?
abstract: Several proteins can traverse biological membranes through protein transduction. Small sections of these proteins (10-16 residues long) are responsible for this. Linking these domains covalently to compounds, peptides, antisense peptide nucleic acids or 40-nm iron beads, or as in-frame fusions with full-length proteins, lets them enter any cell type in a receptor- and transporter-independent fashion. Moreover, several of these fusions, introduced into mice, were delivered to all tissues, even crossing the blood-brain barrier. These domains thus might let us address new questions and even help in the treatment of human disease.
authors.affiliation: Howard Hughes Medical Institute, Depts of Pathology and Medicine, and Barnes-Jewish Hospital, Washington University School of Medicine, 4940 Parkview Place, Campus Box 8022, St Louis, MO 63110, USA.
authors.forename: S R
authors.initials: SR
authors.lastname: Schwarze
authors.forename: K A
authors.initials: KA
authors.lastname: Hruska
authors.forename: S F
authors.initials: SF
authors.lastname: Dowdy
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D001812:Blood-Brain Barrier / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000493:pharmacokinetics*; D011993:Recombinant Fusion Proteins / Q000493:pharmacokinetics
chemical_list: D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins