Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4701
Title: Impact of the peptide sequence on the coordination abilities of albumin-like tripeptides towards Cu2+, Ni2+, Zn2+ ions. Potential albumin-like peptides chelators
Authors: Mlynarz, P.
Valensin, Daniela 
Kociolek, K.
Zabrocki, J.
Kozlowski, J.
Olejnik, H.
Keywords: ALPHA-HYDROXYMETHYLSERINE; BINDING ABILITY; TERNARY COMPLEXES; L-HISTIDINE; COPPER(II); STABILITY; OLIGOPEPTIDES; NICKEL(II); CHEMISTRY; RESIDUE
Issue Date: 2002
Project: None 
Journal: NEW JOURNAL OF CHEMISTRY
Abstract: 
Thermodynamic and spectroscopic studies have shown that the insertion of alpha-hydroxylmethylserine (HmS) residues into the N-terminal peptide motif of human serum albumin results in a very powerful chelating agent for Cu2+ and Ni2+ ions. The insertion of two HmS residues results in the HmS-HmS-His-OH/NH2 sequence, which is the most effective chelating agent based on an albumin-like sequence for both studied metal ions, especially when the C-terminal carboxylate is protected by an amide function.
Description: 
27137
URI: http://hdl.handle.net/20.500.12779/4701
ISSN: 1144-0546
DOI: 10.1039/b107412c
Appears in Collections:Publications

Show full item record

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.