Abstract
Dehydrobutyrine is an amino acid that is present in a range of peptide natural products. Reaction of pentafluoropyridine with threonine and subsequent E1cb-type elimination allowed the preparation of novel dehydrobutyrine-containing amino acids under mild conditions.
Highlights
Dehydroamino acids such as dehydroalanine (Dha, 1) and dehydrobutyrines (Dhb, 2a and 2b) are naturally occurring amino acids that are present in a range of peptides[1] including antimicrobial peptides of the lantibiotic family.[2]
We have shown that pentafluoropyridine (3) reacts with orthogonally protected serine derivatives (e.g., 4 and 5) as a route to generating novel peptide building blocks (6 and 7) (Scheme 1).[10]
In an effort to expand and exploit this observation to access a range of novel dehydrobutyrines potentially
Summary
Dehydroamino acids such as dehydroalanine (Dha, 1) and dehydrobutyrines (Dhb, 2a and 2b) are naturally occurring amino acids that are present in a range of peptides[1] including antimicrobial peptides of the lantibiotic family.[2]. Often the formation of 2a or 2b from threonine requires harsh reaction conditions, and generally involves electron-withdrawing substituents, e.g., Boc or nosyl, at the amino group of the amino acid to increase the acidity of the a-
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