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) |
|---|---|
| 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
Fingerprint
Dive into the research topics of 'Noncovalent multivalent assembly of jun peptides on a leucine zipper dendrimer displaying fos peptides'. Together they form a unique fingerprint.Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS