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A novel reagent, dialkylphosphite, for peptide synthesis
International Journal of Peptide and Protein Research
|May 1, 1991
Summary
A novel dialkylphosphite reagent offers dual function in peptide synthesis for N-protection and C-activation. This method yields unique mass spectrometry cleavage patterns useful for peptide sequencing and conformational analysis.
Area of Science:
- Organic Chemistry
- Peptide Chemistry
- Mass Spectrometry
Background:
- Amino acid protection and activation are crucial steps in peptide synthesis.
- Developing versatile reagents that simplify synthetic procedures is an ongoing challenge.
Purpose of the Study:
- To introduce a novel dialkylphosphite reagent for simultaneous N-protection and C-activation of amino acids.
- To explore the utility of the resulting phosphinyl-protected peptides in mass spectrometry and NMR analysis.
Main Methods:
- Synthesis of N-diisopropyloxyphosphinyl (Dipp) tripeptide esters and N-Dipp-dipeptide acids.
- Analysis using positive ion Fast Atom Bombardment Mass Spectrometry (FAB-MS).
- Characterization using 31P-Nuclear Magnetic Resonance (NMR) spectroscopy.
Main Results:
- Successful preparation of Dipp-protected peptide derivatives.
- Observation of novel, intense N-phosphoryl fragment ions in FAB-MS, with absent C-terminal ions.
- Demonstration of 31P-NMR utility for conformational analysis and racemization assessment.
Conclusions:
- The dialkylphosphite reagent provides a versatile tool for both N-protection and C-activation in peptide synthesis.
- The unique FAB-MS fragmentation patterns offer potential for advanced peptide sequencing.
- 31P-NMR analysis of the dialkyloxyphosphinyl group aids in conformational studies and quality control of peptide coupling.