Issue 2, 1999
From the journal:

Journal of the Chemical Society, Dalton Transactions

Introduction of α-hydroxymethylserine residues in a peptide sequence results in the strongest peptidic, albumin-like, copper(II) chelator known to date

Piotr Młynarz,   Wojciech Bal,   Teresa Kowalik-Jankowska,   Marcin Stasiak,   Mirosław T. Leplawy  and  Henryk Kozłowski  

Abstract

A tripetide amide HmS-HmS-His-NH2 is the strongest peptidic CuII chelator known to date, due to the steric shielding of the chelate plane as well as electronic effects.

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Article information

DOI
https://doi.org/10.1039/A808269C
Article type
Paper

J. Chem. Soc., Dalton Trans., 1999, 109-110

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Introduction of α-hydroxymethylserine residues in a peptide sequence results in the strongest peptidic, albumin-like, copper(II) chelator known to date

P. Młynarz, W. Bal, T. Kowalik-Jankowska, M. Stasiak, M. T. Leplawy and H. Kozłowski, J. Chem. Soc., Dalton Trans., 1999, 109 DOI: 10.1039/A808269C

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