Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/5465
Title: The His-His sequence of the antimicrobial peptide demegen P-113 makes it very attractive ligand for Cu2+
Authors: Kulon, K
Valensin, Daniela 
Kamysz, W
Valensin, Gianni 
Nadolski, P
Porciatti, E
Gaggelli, Elena 
Kozlowski, H.
Keywords: Copper(II) complexes; Peptides; His-pair; Structure; Demegen
Issue Date: 2008
Project: None 
Journal: JOURNAL OF INORGANIC BIOCHEMISTRY
Abstract: 
Histatins are a family of histidine-rich, cationic peptides up to 38 amino acids long. As other antimicrobial peptides histatins exhibit in vitro activity against both bacteria and yeasts. A 12 amino acid amidated fragment of histatin 5, designated P-113 or demegen, has been identified as the smallest fragment retaining antimicrobial activity comparable to the parent compound. Demegen, AKRHHGYKRKFH, has three His and a N-terminal group known to participate in copper ion coordination. In this study potentiometric and spectroscopic (UV–vis, CD, EPR, NMR) measurements were used to evaluate the stability constants, stoichiometry and structures of Cu2+ complexes with demegen P-113 and its analogues in aqueous solution. The main aim of this work was to understand the role of two adjacent histidine residues in metal ion binding. The comparison with results for modified ligands showed that two histydyl residues are basic for complex formation in the 4.5–7 pH range.
Description: 
35053
URI: http://hdl.handle.net/20.500.12779/5465
ISSN: 0162-0134
DOI: 10.1016/j.jinorgbio.2007.12.021
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