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 language | English (US) |
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Pages (from-to) | 3561-3564 |
Number of pages | 4 |
Journal | Organic Letters |
Volume | 6 |
Issue number | 20 |
DOIs | |
State | Published - Sep 30 2004 |
ASJC Scopus subject areas
- Biochemistry
- Physical and Theoretical Chemistry
- Organic Chemistry