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Capreomycin--a polypeptide antitubercular antibiotic with unusual binding properties toward copper(II).
- Source :
-
Journal of inorganic biochemistry [J Inorg Biochem] 2012 Jan; Vol. 106 (1), pp. 111-6. Date of Electronic Publication: 2011 Sep 14. - Publication Year :
- 2012
-
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 α,β-diaminopropionic acid residue at pH around 5. At physiological pH copper(II) ion is coordinated by two deprotonated amide nitrogen atoms of the α,β-diaminopropionic acid, the serine residue as well as the amino function deriving from the β-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 β-ureidodehydroalanine moiety is the fourth donor atom.<br /> (Copyright © 2011 Elsevier Inc. All rights reserved.)
- Subjects :
- Antibiotics, Antitubercular metabolism
Binding Sites
Capreomycin metabolism
Circular Dichroism
Copper metabolism
Kinetics
Magnetic Resonance Spectroscopy
Models, Chemical
Models, Molecular
Molecular Structure
Peptides metabolism
Potentiometry
Protein Binding
Spectrophotometry
beta-Alanine analogs & derivatives
beta-Alanine chemistry
beta-Alanine metabolism
Antibiotics, Antitubercular chemistry
Capreomycin chemistry
Copper chemistry
Peptides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3344
- Volume :
- 106
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Journal of inorganic biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 22112847
- Full Text :
- https://doi.org/10.1016/j.jinorgbio.2011.08.021