Enzymes as reagents in peptide synthesis: enzyme-labile protection for carboxyl groups

Journal Article · Fri Jul 01 04:00:00 EDT 1977 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.74.7.2739· OSTI ID:7220772

Glass, J; Pelzig, M

N-Benzyloxycarbonyl derivatives of isoglutamine and isoasparagine were coupled with arginine methyl ester through the action of dicyclohexylcarbodiimide. The resulting benzyloxycarbonyl derivatives of isoglutaminylarginine methyl ester and isoasparaginylarginine methyl ester were treated with trypsin for removal of the ester groups and then with porcine pancreatic carboxypeptidase B for liberation of arginine and the original benzyloxycarbonyl derivatives of isoglutamine and isoasparagine. This scheme represents a reversible masking of the side-chain carboxyl functions of aspartic and glutamic acid residues. Possible applications of esters and amides of arginine as reversible blocking groups in protein semi-synthesis are discussed along with prospects and strategies for developing related techniques of higher efficiency.

• Research Organization: City Univ. of New York
• OSTI ID: 7220772
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 74:7; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
550500 -- Metabolism
59 BASIC BIOLOGICAL SCIENCES
BIOSYNTHESIS
CARBOXYPEPTIDASE
ENZYMES
ESTERS
HYDROLASES
METABOLISM
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PEPTIDES
PROTEINS
RESIDUES
SYNTHESIS