N-terminal acylation of the SV40 nuclear localization signal peptide enhances its oligonucleotide binding and membrane translocation efficiencies

I. Laczkó, G. Váró, S. Bottka, Zoltán Bálint, Eszter Illyés, E. Vass, Jean Remy Bertrand, Claude Malvy, M. Hollósi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Octanoyl and palmitoyl groups were coupled to the N-terminus of an analog of the SV40 nuclear localization signal peptide, SV126-133(Ser128), to study the effect of the fatty acid chain length on the complex formation with a single-stranded antisense oligodeoxynucleotide (ODN) and on the cellular uptake of the complex. The strongest binding affinity was observed for the palmitoylated peptide, indicating the better accessibility of the positively charged lysyl and arginyl side-chains to the phosphate groups due to the turn structures stabilized by the palmitoyl group. On increase of the peptide to ODN molar ratio (rM), gradual unstacking of the bases was observed, the maximal rate being reached at rM = 10. At rM > 10 restacking of the nucleotide bases was detected and the ODN was completely encapsulated in a liposome-like structure made up of palmitoylated peptides. Cell translocation experiments revealed a highly efficient cell transport of the ODN by palmitoylated SV40 peptide at rM > 10.

Original languageEnglish
Pages (from-to)146-154
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume454
Issue number2
DOIs
Publication statusPublished - Oct 15 2006

Fingerprint

Acylation
Nuclear Localization Signals
Oligodeoxyribonucleotides
Protein Sorting Signals
Oligonucleotides
Membranes
Peptides
Chain length
Liposomes
Fatty Acids
Nucleotides
Phosphates
SV40 nuclear localization peptide
Experiments

Keywords

  • Acylated peptides
  • Antisense oligonucleotide
  • Atomic force microscopy
  • Attenuated total reflection FTIR
  • Cell translocation
  • Circular dichroism
  • Epifluorescence
  • Nuclear localization signal peptide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

N-terminal acylation of the SV40 nuclear localization signal peptide enhances its oligonucleotide binding and membrane translocation efficiencies. / Laczkó, I.; Váró, G.; Bottka, S.; Bálint, Zoltán; Illyés, Eszter; Vass, E.; Bertrand, Jean Remy; Malvy, Claude; Hollósi, M.

In: Archives of Biochemistry and Biophysics, Vol. 454, No. 2, 15.10.2006, p. 146-154.

Research output: Contribution to journalArticle

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AU - Váró, G.

AU - Bottka, S.

AU - Bálint, Zoltán

AU - Illyés, Eszter

AU - Vass, E.

AU - Bertrand, Jean Remy

AU - Malvy, Claude

AU - Hollósi, M.

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