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

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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

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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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