Molecular Biology Reports

, Volume 46, Issue 1, pp 867–885 | Cite as

Potential bio-protective effect of copper compounds: mimicking SOD and peroxidases enzymes and inhibiting acid phosphatase as a target for anti-osteoporotic chemotherapeutics

  • Nancy Martini
  • Juliana E. Parente
  • Franco D´Alessandro
  • Marilin Rey
  • Alberto Rizzi
  • Patricia A. M. Williams
  • Evelina G. FerrerEmail author
Original Article


Copper complexes with transformed methimazole ligand have been synthesized and characterized by elemental analysis, conductivity measurements, thermogravimetric analysis, EPR, FTIR and UV–Vis spectroscopies. Results support their stoichiometries and geometrical structures: [Cu(C4H5N2S)2Cl2]·2H2O(1), [Cu(C8H10N4S)SO4H2O](2) and [Cu(C8H10N4S)SO4](3). ((C4H5N2)2S: bis(l-methylimidazol-2-yl)sulfide; (C4H5N2S)2 = Bis[bis(l-methylimidazol-2-yl)disulfide]) Concurrently, the structurally distinct soluble species corresponding to complexes (1) and (2) were subsequently used in an in vitro investigation of their potential biological properties. In view of their possible pharmaceutical activity, the complexes were in vitro evaluated as phosphatase acid inhibitors. Their radical bio-protective effects were also studied measuring the effect against DPPH and O2•− radicals. Additional catalytic properties as peroxidase mimics were evaluated using Michaelis–Menten kinetic model by means of phenol red and pyrogallol assays. The complexes exhibited catalytic bromination activity and the ability to oxidize pyrogallol substrate indicating that they can be considered as functional models. The relationships between the structures and the in vitro biological activities have also been considered. Serum protein albumin has attracted the greatest interest as drug carrier and the affinity of biological/pharmaceutical compound is relevant to the development of new medicine. In that sense, interaction studies by fluorescence and EPR spectroscopies were performed showing the binding capacity of the complexes.


Copper complexes Phosphatase inhibition Peroxidase-like activity Superoxide dismutase activity 









2,2′-Azinobis(3-ethyl-benzothiazoline-6-sulfonic acid) diammonium salt


Acid phosphatase


Bovine serum albumin




Dimethyl sulfoxide


Fetal calf serum


Buffered saline, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid




Reduced nicotinamide adenine dinucleotide


Nitroblue tetrazolium


Nitrilotriacetic acid


Phenazine methosulfate


Paranitrophenyl phosphate


Tris(hydroxymethyl)aminomethane hydrochloride



This work was supported by CONICET (PIP 0611, PIP 0550), ANPCyT (PICT16-1814, PICT14-1742, PICT17-2186), UNLP (X777), UNL (CAI+D 2016-50420150100070LI) of Argentina. LGN and EGF are Research Fellows of CONICET. JEP and PAMW are Research Fellows of CICPBA, Argentina.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

11033_2018_4542_MOESM1_ESM.docx (5 mb)
Supplementary material 1 (DOCX 5085 KB)


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Copyright information

© Springer Nature B.V. 2018

Authors and Affiliations

  • Nancy Martini
    • 1
  • Juliana E. Parente
    • 1
  • Franco D´Alessandro
    • 1
  • Marilin Rey
    • 2
  • Alberto Rizzi
    • 2
  • Patricia A. M. Williams
    • 1
  • Evelina G. Ferrer
    • 1
    Email author
  1. 1.CEQUINOR, CONICET-CICPBA-UNLP, Faculty of Exact SciencesNational University of La PlataLa PlataArgentina
  2. 2.Physics Department, Faculty of Biochemistry and Biological SciencesNational University of the LitoralSanta FeArgentina

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