Affiliations 

  • 1 Department of Pharmaceutical Chemistry, School of Pharmacy, International Medical University, Bukit Jalil, 57000 Kuala Lumpur, Malaysia. Electronic address: [email protected]
  • 2 Department of Pharmaceutical Chemistry, School of Pharmacy, International Medical University, Bukit Jalil, 57000 Kuala Lumpur, Malaysia; Department of Chemistry, University of Malaya, 50603 Kuala Lumpur, Malaysia. Electronic address: [email protected]
  • 3 Department of Pharmaceutical Chemistry, School of Pharmacy, International Medical University, Bukit Jalil, 57000 Kuala Lumpur, Malaysia. Electronic address: [email protected]
  • 4 Department of Pharmaceutical Chemistry, School of Pharmacy, International Medical University, Bukit Jalil, 57000 Kuala Lumpur, Malaysia. Electronic address: [email protected]
  • 5 Faculty of Science, Universiti Tunku Abdul Rahman, 31900 Kampar, Perak, Malaysia. Electronic address: [email protected]
  • 6 Department of Chemistry, University of Malaya, 50603 Kuala Lumpur, Malaysia. Electronic address: [email protected]
  • 7 Department of Biological Sciences, Sunway University, 47500 Bandar Sunway, Malaysia. Electronic address: [email protected]
J Inorg Biochem, 2016 07;160:1-11.
PMID: 27105312 DOI: 10.1016/j.jinorgbio.2016.04.003

Abstract

Like chiral organic drugs, the chemical and biological properties of metal complexes can be dependent on chirality. Two pairs of [Cu(phen)(ala)(H2O)]X·xH2O (phen=1.10-phenanthroline: X=NO3(-); ala: l-alanine (l-ala), 1 and d-alanine (d-ala) 2; and (X=Cl(-); ala: l-ala, 3 and d-ala, 4) complex salts (x=number of lattice water molecules) have been synthesized and characterized. The crystal structure of 3 has been determined. The same pair of enantiomeric species, viz. [Cu(phen)(l-ala)(H2O)](+) and [Cu(phen)(d-ala)(H2O)](+), have been identified to be present in the aqueous solutions of both 1 and 3, and in those of both 2 and 4 respectively. Both 3 and 4 bind more strongly to ds(AT)6 than ds(CG)6. There is no or insignificant effect of the chirality of 3 and 4 on the production of hydroxyl radicals, binding to deoxyribonucleic acid from calf thymus (CT-DNA), ds(CG)6, G-quadruplex and 17-base pair duplex, and inhibition of both topoisomerase I and proteasome. Among the three proteasome proteolytic sites, the trypsin-like site is inhibited most strongly by these complexes. However, the chirality of 3 and 4 does affect the number of restriction enzymes inhibited, and their binding constants towards ds(AT)6 and serum albumin.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.