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Structural Characterization and Antimicrobial Activity of the Zn(II) Complex with P113 (Demegen), a Derivative of Histatin 5

Authorized Users Only
2010
Authors
Porciatti, Elena
Milenković, Marina
Gaggelli, Elena
Valensin, Gianni
Kozlowski, Henryk
Kamysz, Wojciech
Valensin, Daniela
Article (Published version)
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Abstract
Zinc binding to P113 (or demegen), a 12 amino acid (AKRHHGYKRKFH-NH2) fragment of histatin 5, was investigated by means of NMR and CD techniques, yielding delineation of the metal binding site and the 3D structure of the complex in water and in DMSO as well. The three His imidazole and the N-terminus nitrogens were found to act as the zinc coordinating atoms. A comparison with the previously reported Cu(II)-P113 complex disclosed that the two structures were rather diverse, in spite of an identical donor set. The two complexes were also tested for their antimicrobial activity in vitro against seven bacteria and two yeast strains: a minor activity of both complexes vs that of free ligand was given evidence, suggesting both metal ions may possibly play a negative role in vivo.
Source:
Inorganic Chemistry, 2010, 49, 19, 8690-8698
Publisher:
  • Amer Chemical Soc, Washington
Projects:
  • CIRMMP (Consorzio Interuniversitario Risonanze Magnetiche di Metalloproteine Paramagnetiche)

DOI: 10.1021/ic902547t

ISSN: 0020-1669

PubMed: 20815365

WoS: 000282084600011

Scopus: 2-s2.0-77957254923
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URI
http://farfar.pharmacy.bg.ac.rs/handle/123456789/1328
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  • Radovi istraživača / Researchers’ publications
Institution
Pharmacy

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