Noncovalent multivalent assembly of jun peptides on a leucine zipper dendrimer displaying fos peptides

Min Zhou, Indraneel Ghosh

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

(Chemical Equation Presented) The synthesis and characterization of a new leucine-zipper dendrimer (LZD) is reported that displays four copies of the peptide corresponding to the coiled-coiled dimerization domain of Fos. Circular dichroism spectroscopy, fluorescence titration, and sedimentation equilibrium experiments demonstrate that Fos-LZD can noncovalently assemble four copies of the peptide corresponding to the coiled-coil domain of Jun. This work provides the basis for the future construction of noncovalently assembled multivalent protein assemblies displaying any protein of interest.

Original languageEnglish (US)
Pages (from-to)3561-3564
Number of pages4
JournalOrganic Letters
Volume6
Issue number20
DOIs
StatePublished - Sep 30 2004

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zippers
Dendrimers
Leucine Zippers
leucine
dendrimers
peptides
assembly
Circular dichroism spectroscopy
proteins
Peptides
Dimerization
Fluorescence Spectrometry
dimerization
Circular Dichroism
Titration
Sedimentation
titration
assemblies
dichroism
Proteins

ASJC Scopus subject areas

  • Molecular Medicine

Cite this

Noncovalent multivalent assembly of jun peptides on a leucine zipper dendrimer displaying fos peptides. / Zhou, Min; Ghosh, Indraneel.

In: Organic Letters, Vol. 6, No. 20, 30.09.2004, p. 3561-3564.

Research output: Contribution to journalArticle

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