Synthesis and Utility of β-Selenophenylalanine and β-Selenoleucine in Diselenide–Selenoester Ligation
- Resource Type
- Authors
- Bhavesh Premdjee; Richard J. Payne; Xiaoyi Wang; Leo Corcilius
- Source
- The Journal of Organic Chemistry. 85:1567-1578
- Subject
- chemistry.chemical_classification
Aldehydes
010405 organic chemistry
Stereochemistry
Chemistry
Phenylalanine
Organic Chemistry
Proteins
Peptide
010402 general chemistry
01 natural sciences
Aldehyde
0104 chemical sciences
Amino acid
Diselenide
Interferon
medicine
Leucine
Peptides
Ligation
Protein Binding
medicine.drug
- Language
- ISSN
- 1520-6904
0022-3263
The synthesis of suitably protected β-selenophenylalanine and β-selenoleucine amino acids was accomplished from Garner's aldehyde as a common starting point. These selenoamino acids were incorporated into model peptides and shown to facilitate rapid diselenide-selenoester ligation (DSL) with peptide selenoesters which, when coupled with in situ deselenization, afforded native peptide products. The utility of one-pot DSL-deselenization chemistry at phenylalanine and leucine was demonstrated through the rapid synthesis of a glycosylated interferon-γ fragment and the chemokine-binding protein UL22A, respectively.