Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide

K. Kilk, Mazin Magzoub, M. Pooga, L. E.G. Eriksson, U. Langel, A. Gräslund

    Research output: Contribution to journalArticle

    Abstract

    Cellular translocation into a human Bowes melanoma cell line was investigated and compared for penetratin and pIsl, two peptides that correspond to the third helices of the related homeodomains, from the Antennapedia transcription factor of Drosophila and the rat insulin-1 gene enhancer protein, respectively. Both biotinylated peptides internalized into the cells with similar efficacy, yielding an analogous intracellular distribution. When a large cargo protein, 63 kDa avidin, was coupled to either peptide, efficient cellular uptake for both the peptide-protein complexes was observed. The interactions between each peptide and SDS micelles were studied by fluorescence spectroscopy and acrylamide quenching of the intrinsic tryptophan (Trp) fluorescence. Both peptides interacted strongly and almost identically with the membrane mimicking environment. Compared to penetratin, the new transport peptide pIsl has only one Trp residue, which simplifies the interpretation of the fluorescence spectra and in addition has a native Cys residue, which may be used for alternative coupling reactions of cargoes of different character.

    Original languageEnglish (US)
    Pages (from-to)911-916
    Number of pages6
    JournalBioconjugate Chemistry
    Volume12
    Issue number6
    DOIs
    StatePublished - Dec 29 2001

    Fingerprint

    Peptides
    Proteins
    Tryptophan
    Fluorescence
    Transcription factors
    Avidin
    Acrylamide
    Insulin
    Fluorescence Spectrometry
    Fluorescence spectroscopy
    Micelles
    penetratin
    Drosophila
    Rats
    Quenching
    Melanoma
    Transcription Factors
    Genes
    Cells
    Membranes

    ASJC Scopus subject areas

    • Biotechnology
    • Bioengineering
    • Biomedical Engineering
    • Pharmacology
    • Pharmaceutical Science
    • Organic Chemistry

    Cite this

    Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide. / Kilk, K.; Magzoub, Mazin; Pooga, M.; Eriksson, L. E.G.; Langel, U.; Gräslund, A.

    In: Bioconjugate Chemistry, Vol. 12, No. 6, 29.12.2001, p. 911-916.

    Research output: Contribution to journalArticle

    Kilk, K. ; Magzoub, Mazin ; Pooga, M. ; Eriksson, L. E.G. ; Langel, U. ; Gräslund, A. / Cellular internalization of a cargo complex with a novel peptide derived from the third helix of the islet-1 homeodomain. Comparison with the penetratin peptide. In: Bioconjugate Chemistry. 2001 ; Vol. 12, No. 6. pp. 911-916.
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    abstract = "Cellular translocation into a human Bowes melanoma cell line was investigated and compared for penetratin and pIsl, two peptides that correspond to the third helices of the related homeodomains, from the Antennapedia transcription factor of Drosophila and the rat insulin-1 gene enhancer protein, respectively. Both biotinylated peptides internalized into the cells with similar efficacy, yielding an analogous intracellular distribution. When a large cargo protein, 63 kDa avidin, was coupled to either peptide, efficient cellular uptake for both the peptide-protein complexes was observed. The interactions between each peptide and SDS micelles were studied by fluorescence spectroscopy and acrylamide quenching of the intrinsic tryptophan (Trp) fluorescence. Both peptides interacted strongly and almost identically with the membrane mimicking environment. Compared to penetratin, the new transport peptide pIsl has only one Trp residue, which simplifies the interpretation of the fluorescence spectra and in addition has a native Cys residue, which may be used for alternative coupling reactions of cargoes of different character.",
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    AU - Kilk, K.

    AU - Magzoub, Mazin

    AU - Pooga, M.

    AU - Eriksson, L. E.G.

    AU - Langel, U.

    AU - Gräslund, A.

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    AB - Cellular translocation into a human Bowes melanoma cell line was investigated and compared for penetratin and pIsl, two peptides that correspond to the third helices of the related homeodomains, from the Antennapedia transcription factor of Drosophila and the rat insulin-1 gene enhancer protein, respectively. Both biotinylated peptides internalized into the cells with similar efficacy, yielding an analogous intracellular distribution. When a large cargo protein, 63 kDa avidin, was coupled to either peptide, efficient cellular uptake for both the peptide-protein complexes was observed. The interactions between each peptide and SDS micelles were studied by fluorescence spectroscopy and acrylamide quenching of the intrinsic tryptophan (Trp) fluorescence. Both peptides interacted strongly and almost identically with the membrane mimicking environment. Compared to penetratin, the new transport peptide pIsl has only one Trp residue, which simplifies the interpretation of the fluorescence spectra and in addition has a native Cys residue, which may be used for alternative coupling reactions of cargoes of different character.

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