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Published August 1990 | public
Journal Article

Reagents and methods for the solid-phase synthesis of protein-EDTA for use in affinity cleaving

Abstract

Synthetic procedures for the introduction of the metal chelator ethylenediaminetetraacetic acid (EDTA) at unique amino acid positions of proteins by solid-phase methods are described. Two protected derivatives of EDTA compatible with Merrifield solid-phase protein synthesis employing N-tert-butyloxycarbonyl- (Boc-) protected amino acids were developed. The first reagent is a dipeptide with three of four carboxyl groups of EDTA protected as benzyl esters and the fourth coupled to a γ-aminobutanoic acid linker, referred to as tribenzyl-EDTA-CABA (BEG). A second reagent is the tricyclohexyl ester of EDTA, TCE. BEG and TCE allow the modification of the NH_2 terminus and/or lysine side chains of resin-bound peptides and proteins. Upon deprotection and cleavage from the resin, a protein is produced with EDTA at a defined amino acid position. The availability of protein-EDTA conjugates extends the affinity cleaving method to the study of protein-DNA complexes in solution.

Additional Information

© 1990 American Chemical Society. Received February 5, 1990. We are grateful for generous support from the DARPA University Research Initiative Program, Merck, an NSF predoctoral fellowship to J.H.G., and NIH traineeships to J.P.S. and D.P.M.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023