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Dalton Transactions

The leading European journal for inorganic and organometallic chemistry




Paper

J. Chem. Soc., Dalton Trans., 1999, 109 - 110, DOI: 10.1039/a808269c


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

Piotr Mynarz, Wojciech Bal, Teresa Kowalik-Jankowska, Marcin Stasiak, Mirosaw T. Leplawy and Henryk Kozowski


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.