SELECTIVE ENZYMATIC REMOVAL OF PROTECTING GROUPS - N-HEPTYL ESTERS AS CARBOXY 
PROTECTING FUNCTIONS IN PEPTIDE-SYNTHESIS

BRAUN, P; Waldmann, Herbert; VOGT, W; KUNZ, H

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SELECTIVE ENZYMATIC REMOVAL OF PROTECTING GROUPS - N-HEPTYL ESTERS AS CARBOXY PROTECTING FUNCTIONS IN PEPTIDE-SYNTHESIS

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Waldmann, Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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BRAUN, P., Waldmann, H., VOGT, W., & KUNZ, H. (1991). SELECTIVE ENZYMATIC REMOVAL OF PROTECTING GROUPS - N-HEPTYL ESTERS AS CARBOXY PROTECTING FUNCTIONS IN PEPTIDE-SYNTHESIS. LIEBIGS ANNALEN DER CHEMIE, (2), 165-170.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-9AD3-7

Abstract

Amino acid (Hep) esters are accessible as generally crystalline hydro tosylates 3 from the amino acids by azeotropic esterification with 1-heptanol in high yields. They can be condensed with Z-, Boc-, and Aloc-protected amino acids to give the dipeptides 7-9 in the presence of 1-ethoxycarbonyl-2-ethoxy-1,2-dihydroquinoline (EEDQ). From the fully protected dipeptides the N-terminal protecting groups are cleaved by chemical methods without affecting the Hep esters. On the other hand, the heptyl esters can be hydrolyzed under mild conditions (pH = 7.0, 37-degrees-C) and with high yields by means of a lipase from Rhizopus niveus without attacking the N-terminal urethane groups or the peptide bonds.