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DNA Cleavage Study Using Copper (II)-GlyAibHis: A Tripeptide Complex Based on ATCUN Peptide Motifs

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Abstract:

Development of new chemical nucleases is a matter of great interest because of their extensive use in biotechnology and as therapeutic agents. The ATCUN (amino terminal Cu(II) and Ni(II) binding) is a peptide motif that occurs naturally in the serum albumins. The similar peptide motif (GlyAibHis) having unnatural amino acid Aib (α- aminoisobutyric acid) was synthesized and its Cu(II) complex was characterized by ESI-MS and spectrophotometry studies. The reactivity of this complex toward DNA cleavage has been investigated. Cu(II)-GlyAibHis shows the DNA cleavage only in presence of mild oxidizing agents like ascorbate by an oxidative mechanism rather than hydrolytic and follows the pseudo first order kinetics (Kobs = 0.085 min-1). The non-hydrolytic mechanism was further supported by the hydrolysis of pNPP which followed the pseudo first order kinetics (Kobs = 1.98 x 10-2 min-1) having no pH effect.





Keywords: Calf thymus DNA; Circular Dichroism; Ester Hydrolysis; Solid phase synthesis; para-nitrophenylphosphate

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986608783330378

Publication date: January 1, 2008

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
ben/ppl/2008/00000015/00000001/art00003
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