Noncovalent multivalent assembly of jun peptides on a leucine zipper dendrimer displaying fos peptides.
[reaction: see text] 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.
Zhou
Min
M
Department of Chemistry, University of Arizona, Tucson, Arizona 85721, USA.
Ghosh
Indraneel
I
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D016350:Leucine Zippers; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D016760:Proto-Oncogene Proteins c-fos / Q000138:chemical synthesis*; D016755:Proto-Oncogene Proteins c-jun / Q000138:chemical synthesis*
D010455:Peptides; D016760:Proto-Oncogene Proteins c-fos; D016755:Proto-Oncogene Proteins c-jun