Facile solid phase peptide synthesis with a Re-lysine conjugate generated via a one-pot procedure
Kullapa Chanawanno1, Joel Caporoso, Vinay Kondeti
1Department of Chemistry, University of Akron, Akron, OH 44325-3601, USA. ziegler@uakron.edu.
Dalton Transactions (Cambridge, England : 2003)
|May 31, 2014
Summary
Researchers created a rhenium(I) tricarbonyl-modified lysine for solid-phase peptide synthesis. This new building block was attached to a neurotensin fragment, showing cellular uptake in endothelial cells.
Area of Science:
- Bioinorganic Chemistry
- Organic Synthesis
- Cell Biology
Background:
- Solid-phase peptide synthesis (SPPS) is crucial for creating peptides.
- Incorporating non-canonical amino acids can expand peptide functionality.
- Rhenium(I) tricarbonyl complexes offer unique photophysical and radiolabeling properties.
Purpose of the Study:
- To synthesize a novel rhenium(I) tricarbonyl-modified lysine for SPPS.
- To demonstrate the utility of this modified amino acid in peptide synthesis.
- To evaluate the cellular uptake of a peptide containing this modification.
Main Methods:
- One-pot Schiff base formation for amino acid modification.
- Solid-phase peptide synthesis to incorporate the modified lysine.
- Attachment to a neurotensin fragment.
- Cellular uptake studies using human umbilical vascular endothelial cells.
Main Results:
- Successful synthesis of a Re(CO)3-modified lysine.
- Demonstrated its compatibility with SPPS.
- Successfully attached the modified lysine to a neurotensin peptide fragment.
- Observed cellular uptake of the modified peptide into endothelial cells.
Conclusions:
- A novel Re(CO)3-modified lysine is available for SPPS.
- This modified amino acid can be incorporated into peptides.
- The resulting peptides show potential for cellular delivery applications.
