Analysis of the interaction with biomembrane models of the HAV-VP3(101-121) sequence conjugated to synthetic branched chain polypeptide carriers with a poly[L-lysine] backbone

M. Garcí, I. Nagy, M. A. Alsina, G. Mező, F. Reig, F. Hudecz, I. Haro

Research output: Article

14 Citations (Scopus)

Abstract

The conjugation of the [Abu105,109 ] VP3(101-121) peptide sequence from the VP3 capsid protein of hepatitis A virus to synthetic branched polypeptide carriers is described. The establishment of either a disulfide or an amide bond between the peptide and the carrier molecules is reported. The interaction of VP3 conjugates with dipalmitoylphosphatidylcholine (DPPC) mono- and bilayers was studied, and the influence of the different hydrophilicities and peptide orientations on the conjugates is discussed. Results showed an increased interaction with biomembrane models due to the conjugation of VP3 peptide to the described macromolecular structures.

Original languageEnglish
Pages (from-to)1861-1869
Number of pages9
JournalLangmuir
Volume14
Issue number7
Publication statusPublished - márc. 31 1998

Fingerprint

lysine
Polypeptides
polypeptides
Peptides
Lysine
peptides
conjugation
interactions
hepatitis
Hydrophilicity
disulfides
viruses
1,2-Dipalmitoylphosphatidylcholine
Viruses
Amides
amides
Capsid Proteins
Monolayers
Disulfides
proteins

ASJC Scopus subject areas

  • Colloid and Surface Chemistry
  • Physical and Theoretical Chemistry

Cite this

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abstract = "The conjugation of the [Abu105,109 ] VP3(101-121) peptide sequence from the VP3 capsid protein of hepatitis A virus to synthetic branched polypeptide carriers is described. The establishment of either a disulfide or an amide bond between the peptide and the carrier molecules is reported. The interaction of VP3 conjugates with dipalmitoylphosphatidylcholine (DPPC) mono- and bilayers was studied, and the influence of the different hydrophilicities and peptide orientations on the conjugates is discussed. Results showed an increased interaction with biomembrane models due to the conjugation of VP3 peptide to the described macromolecular structures.",
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T1 - Analysis of the interaction with biomembrane models of the HAV-VP3(101-121) sequence conjugated to synthetic branched chain polypeptide carriers with a poly[L-lysine] backbone

AU - Garcí, M.

AU - Nagy, I.

AU - Alsina, M. A.

AU - Mező, G.

AU - Reig, F.

AU - Hudecz, F.

AU - Haro, I.

PY - 1998/3/31

Y1 - 1998/3/31

N2 - The conjugation of the [Abu105,109 ] VP3(101-121) peptide sequence from the VP3 capsid protein of hepatitis A virus to synthetic branched polypeptide carriers is described. The establishment of either a disulfide or an amide bond between the peptide and the carrier molecules is reported. The interaction of VP3 conjugates with dipalmitoylphosphatidylcholine (DPPC) mono- and bilayers was studied, and the influence of the different hydrophilicities and peptide orientations on the conjugates is discussed. Results showed an increased interaction with biomembrane models due to the conjugation of VP3 peptide to the described macromolecular structures.

AB - The conjugation of the [Abu105,109 ] VP3(101-121) peptide sequence from the VP3 capsid protein of hepatitis A virus to synthetic branched polypeptide carriers is described. The establishment of either a disulfide or an amide bond between the peptide and the carrier molecules is reported. The interaction of VP3 conjugates with dipalmitoylphosphatidylcholine (DPPC) mono- and bilayers was studied, and the influence of the different hydrophilicities and peptide orientations on the conjugates is discussed. Results showed an increased interaction with biomembrane models due to the conjugation of VP3 peptide to the described macromolecular structures.

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