Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6082
Title: Capreomycin - A polypeptide antitubercular antibiotic with unusual binding properties toward copper(II)
Authors: Stokowa, K
Szczepanik, W
Gaggelli, Elena 
Gaggelli, Nicola 
Valensin, Gianni 
Jezowska Bojczuk, M.
Issue Date: 2012
Project: None 
Journal: JOURNAL OF INORGANIC BIOCHEMISTRY
Abstract: 
Capreomycin is an important therapeutic agent having intriguing and diverse molecular features. Its polypeptidic structure rich in nitrogen donors makes the drug a promising chelating agent for a number of transition metal ions, especially for copper(II). The results of the model investigational studies suggest that capreomycin anchors Cu(2+) ion with an amino function of the alpha,beta-diaminopropionic acid residue at pH around 5. At physiological pH copper(II) ion is coordinated by two deprotonated amide nitrogen atoms of the alpha,beta-diaminopropionic acid, the serine residue as well as the amino function deriving from the beta-lysine. Above that pH value we observe a rearrangement within the coordination sphere leading to movement of Cu(2+) to the center of the peptide ring with concurrent coordination of four nitrogen donors. Spin-lattice relaxation enhancements and potentiometric measurements clearly indicate that deprotonated amide nitrogen atom from the beta-ureidodehydroalanine moiety is the fourth donor atom.
Description: 
42347
URI: http://hdl.handle.net/20.500.12779/6082
ISSN: 0162-0134
DOI: 10.1016/j.jinorgbio.2011.08.021
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