New enzymatic protecting group techniques for the construction of peptides and glycopeptides.
The use of non-proteases for the selective removal of protecting groups from peptides and glycopeptides is described. The N-terminal deprotection of peptides can be achieved by the hydrolysis of the phenylacetyl (PhAc) amide blocking group catalyzed by penicillin G acylase. On the other hand, the lipase-mediated hydrolysis of n-heptyl (Hep) and 2-bromoethyl esters allows for the liberation of the C-terminal carboxy group. The selective C-terminal deprotection can be applied advantageously for the construction of acid- and base-sensitive polyfunctional O-glycopeptides. In all cases the enzymatic reactions are completely selective and proceed under mildest conditions (pH 7-8, r.t. to 37 degrees C) without damaging the various other functionalities present in the complex substrates.
Waldmann
H
H
Johannes-Gutenberg-Universität Mainz, Institut für Organische Chemie.
Braun
P
P
Kunz
H
H
D000595:Amino Acid Sequence; D002240:Carbohydrate Sequence; D004151:Dipeptides / Q000138:chemical synthesis / Q000737:chemistry; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000737:chemistry; D008049:Lipase / Q000737:chemistry; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010399:Penicillin Amidase / Q000737:chemistry; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry
D004151:Dipeptides; D006020:Glycopeptides; D010455:Peptides; D008049:Lipase; D010399:Penicillin Amidase