Linked Life Data

18262278

Source:http://linkedlifedata.com/resource/pubmed/id/18262278

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-3-17
pubmed:abstractText
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 Cu(2+) 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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
960-72
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The His-His sequence of the antimicrobial peptide demegen P-113 makes it very attractive ligand for Cu2+.
pubmed:affiliation
Faculty of Chemistry, University of Wroc?aw, F. Joliot-Curie 14, 50-383 Wroc?aw, Poland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't