Installation of Metal-Binding Functionality at Lysine Residues via Azide-Alkyne "Click Chemistry"
- ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)
- Matthew Baucom (Creator)
- Institution
- East Carolina University (ECU )
- Web Site: http://www.ecu.edu/lib/
Abstract: A novel non-natural amino acid designed to bind divalent metal ions, dubbed Lys(PYRIT), was prepared in a “click reaction” by treating Fmoc-Lys(N3)-OH with 2-ethynylpyridine and Cu(I). It was incorporated into a 12-residue peptide using standard Fmoc solid phase synthesis protocols. Multiple spectroscopic techniques (NMR, ESI-QToF-MS, UV-vis, and CD) confirm that the PYRIdinyl/Triazolyl side-chain binds Zn(II) and Cu(II) in the presence of competing natural residues such as histidine and glutamic acid. It remains unclear whether metal ions mediate the oligomerization of the Y2K PYRIT peptide, as is believed to be important in neurodegenerative diseases.
Additional Information
- Publication
- Thesis
- Baucom, Matthew. (2015). Installation of Metal-Binding Functionality at Lysine Residues via Azide-Alkyne "Click Chemistry". Unpublished manuscript, Honors College, East Carolina University, Greenville, N.C.
- Language: English
- Date: 2015
- Keywords
- Amino acids, Metal binding, Click chemistry, Alzheimer's disease
Title | Location & Link | Type of Relationship |
Installation of Metal-Binding Functionality at Lysine Residues via Azide-Alkyne "Click Chemistry" | http://hdl.handle.net/10342/4795 | The described resource references, cites, or otherwise points to the related resource. |