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  • 1. Jones, Sarah
    et al.
    Holm, Tina
    Stockholm University, Faculty of Science, Department of Neurochemistry.
    Mäger, Imre
    Langel, Ülo
    Stockholm University, Faculty of Science, Department of Neurochemistry. University of Tartu, Estonia.
    Howl, John
    Characterisation of bioactive cell penetrating peptides from human Cytochrome c: protein mimicry and the development of a novel apoptogenic agent2010In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 17, no 7, p. 735-744Article in journal (Refereed)
    Abstract [en]

    Cell penetrating peptides (CPPs) with intrinsic biological activities offer a novel strategy for the modulation of intracellular events. QSAR analysis identified CPPs within human cytochrome c. Two such sequences, Cyt c77–101 and Cyt c86–101, induced tumor cell apoptosis, thus mimicking the role of Cyt c as a key regulator of programmed cell death. Quantitative analyses confirmed that Cyt c77–101 is an extremely efficient CPP. Thus, Cyt c77–101 was selected for modification to incorporate target-specific peptidyl motifs. Chimeric N-terminal extension with a target mimetic of FG nucleoporins significantly enhanced the apoptogenic potency of Cyt c77–101 to a concentration readily achievable in vivo. Moreover, this construct, Nup153-Cyt c, facilitates the dramatic redistribution of nuclear pore complex proteins and thus propounds the nuclear pore complex as a novel target for the therapeutic induction of apoptosis.

  • 2. Tanaka, Gen
    et al.
    Nakase, Ikuhiko
    Fukuda, Yasunori
    Masuda, Ryo
    Oishi, Shinya
    Shimura, Kazuya
    Kawaguchi, Yoshimasa
    Takatani-Nakase, Tomoka
    Langel, Ülo
    Stockholm University, Faculty of Science, Department of Neurochemistry.
    Gräslund, Astrid
    Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
    Okawa, Katsuya
    Matsuoka, Masao
    Fujii, Nobutaka
    Hatanaka, Yasumaru
    Futaki, Shiroh
    CXCR4 Stimulates Macropinocytosis: Implications for Cellular Uptake of Arginine-Rich Cell-Penetrating Peptides and HIV2012In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 19, no 11, p. 1437-1446Article in journal (Refereed)
    Abstract [en]

    CXCR4 is a coreceptor of HIV-1 infection in host cells. Through a photocrosslinking study to identify receptors involved in internalization of oligoarginine cell-penetrating peptides (CPPs), we found that CXCR4 serves as a receptor that stimulates macropinocytic uptake of the arginine 12-mer peptide (R12) but not of the 8-mer. We also found that stimulating CXCR4 with its intrinsic ligands, stromal cell-derived factor 1α and HIV-1 envelope glycoprotein 120, induced macropinocytosis. R12 had activity to prevent viral infection for HIV-1(IIIB), a subtype of HIV-1 that uses CXCR4 as a coreceptor for entry into susceptible cells, whereas the addition of a macropinocytosis inhibitor, dimethylamiloride, resulted in enhancement of viral infection. The present study shows that CXCR4 triggers macropinocytosis, which may have implications for the cellular uptake of oligoarginine CPPs and internalization of HIV.

  • 3. Verdurmen, Wouter P. R.
    et al.
    Bovee-Geurts, Petra H.
    Wadhwani, Parvesh
    Ulrich, Anne S.
    Hällbrink, Mattias
    Stockholm University, Faculty of Science, Department of Neurochemistry.
    van Kuppevelt, Toin H.
    Brock, Roland
    Preferential Uptake of L- versus D-Amino Acid Cell-Penetrating Peptides in a Cell Type-Dependent Manner2011In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 18, no 8, p. 1000-1010Article in journal (Refereed)
    Abstract [en]

    The use of protease-resistant D-peptides is a prominent strategy for overcoming proteolytic sensitivity in the use of cell-penetrating peptides (CPPs) as delivery vectors. So far, no major differences have been reported for the uptake of L- and D-peptides. Here we report that cationic L-CPPs are taken up more efficiently than their D-counterparts in MC57 fibrosarcoma and He La cells but not in Jurkat T leukemia cells. Reduced uptake of D-peptides co-occurred with persistent binding to heparan sulfates (HS) at the plasma membrane. In vitro binding studies of Land D-peptides with HS indicated similar binding affinities. Our results identify two key events in the uptake of CPPs: binding to HS chains and the initiation of internalization. Only the second event depends on the chirality of the CPP. This knowledge may be exploited for a stereochemistry-dependent preferential targeting of cells.

  • 4. Zhang, Wei
    et al.
    Modén, Olof
    Tars, Kaspars
    Mannervik, Bengt
    Stockholm University, Faculty of Science, Department of Neurochemistry. Uppsala University, Sweden.
    Structure-Based Redesign of GST A2-2 for Enhanced Catalytic Efficiency with Azathioprine2012In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 19, no 3, p. 414-421Article in journal (Refereed)
    Abstract [en]

    Glutathione transferase (GST) A2-2 is the most efficient human enzyme in the biotransformation of the prodrug azathioprine (Aza). The activation of Aza has therapeutic potential for possible use of GSTs in targeted enzyme-prodrug treatment of diseases. Based on the assumed catalytic mechanism and computational docking of Aza to the active site of the enzyme, active-site residues were selected for construction of focused mutant libraries, which were thereafter screened for Aza activity. Mutants with elevated Aza activity were identified, DNA sequenced, and the proteins purified. The two most active mutants showed up to 70-fold higher catalytic efficiency than the parental GST A2-2. The structure of the most active triple mutant (L107G/L108D/F222H) enzyme was determined by X-ray crystallography demonstrating significant changes in the topography of the active site facilitating productive binding of Aza as a substrate.

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