Acetylene-Mediated Borophosphene Dirac Materials as Efficient Anode Materials for Lithium-Ion Batteries.

Generally, graphynes have been generated by the insertion of acetylenic content (-C≡C-) in the graphene network in different ratios. Also, several aesthetically pleasing architectures of two-dimensional (2D) flatlands have been reported with the incorporation of acetylenic linkers between the heteroatomic constituents. Prompted by the experimental realization of boron phosphide, which has provided new insights on the boron-pnictogen family, we have modelled novel forms of acetylene-mediated borophosphene nanosheets by joining the orthorhombic borophosphene stripes with different widths and with different atomic constituents using acetylenic linkers. Structural stabilities and properties of these novel forms have been assessed using first-principles calculations. Investigation of electronic band structure elucidates that all the novel forms show the linear band crossing closer to the Fermi level at Dirac point with distorted Dirac cones. The linearity in the hole and electronic bands impose the high Fermi velocity to the charge carriers close to that of graphene. Finally, we have also unravelled the propitious features of acetylene-mediated borophosphene nanosheets as anodes in Li-ion batteries.

Studies on stabilization of collagen using Cr-doped polydopamine complex.

The stabilization of collagen using different small molecules have been explored for the development of biomaterials. One of the most studied molecules in biomaterials research is polydopamine (PDA) due to its ability to bind to different substrates that ranges from metal surface to collagen. Similarly, in leather tanning, chromium has been an extensively used metal ion as it binds strongly with collagen and enhances its stability. However, as per regulatory authority, the presence of chromium in leather has been restricted to minimum level. Here, we studied the application of chromium doped polydopamine (Cr-PDA) complex as collagen stabilizing agent. The preparation and characterization of Cr-PDA were confirmed using FE-SEM, DLS and FT-IR techniques. Cr-PDA did not alter the triple helical structure of collagen as evidenced from the CD spectral data. Cr-PDA delays the fibrillation in collagen compared to collagen or PDA alone. Calorimetric data shows the enhanced stability of collagen when treated with Cr-PDA compared to collagen control but lesser than PDA alone. Viscometry studies have shown that Cr-PDA reduces the viscosity of collagen compared to PDA or collagen alone. Contact angle studies showed that PDA and Cr-PDA imparts more hydrophobicity to collagen compared to control. Tensile strength studies showed that addition of Cr-PDA or PDA increases the tensile strength of the collagen fiber. The present study on stabilization of collagen using Cr-PDA might be helpful in development of crosslinking agents with eco-friendly approach.

Physico-chemical characterization studies of collagen labelled with Ru(II) polypyridyl complex.

The rich luminescence behaviour exerted by transition metal complexes has found significant role in the development of biomolecular and cellular probes. The conjugation of fluorophore to a protein has its own advantage over the label-free system due to its high sensitivity. While numerous proteins have been labelled with either organic or inorganic fluorophores, the conjugation of luminescent transition metal complexes with collagen has not yet been attempted. Here, in this study, the conjugation of a Ru(II) polypyridyl complex with collagen was carried out and its physico-chemical characterization was studied. The conjugation of Ru(II) to collagen was characterized by UV-Visible, fluorescence and ATR-FT-IR spectroscopy. The conjugation of Ru(II) did not alter the triple helical structure of the collagen as evidenced from CD spectral data. The luminescence behaviour of the Ru-tagged collagen was found to be similar to that of the commercially available fluorescein isothiocyanate (FITC) tagged collagen with increase in luminescence upon addition of collagenase. Gel-based collagenase assay showed that the digestion of collagen can be vizualized using UV light due to intrinsic fluorophore tag without carrying out the staining-destaining processes. Energy dispersive X-Ray analysis (EDAX) confirms the presence of Ru in Ru-collagen fibrils. To the best of our knowledge, this is the first report on the conjugation of a Ru(II) complex with the fibrous protein collagen that exhibits similar property as of FITC-collagen and can be used as an alternative.

Understanding the ancillary ligand effect on luminescent cyclometalated Ir(III) complex as a reporter for 2-acetylaminofluorene DNA(AAF-dG) adduct.

Mutagenic agents such as aromatic amines undergo metabolic activation and produce DNA adducts at C8 position of guanine bases. N-2-acetylaminofluorene (AAF) generates different mutational outcomes when placed at G1, G2, and G3 of a NarI sequence (-G1G2CG3CC/T-). These outcomes are dictated by the conformations adopted by these adducts. Detection of such lesions is of considerable interest owing to their hazardous effects. Here, we report the synthesis of three cyclometalated [Ir(L)2dppz]+ complexes (L = 2-phenylpyridine (ppy) 1; benzo[h]quinoline (bhq) 2; 2-phenylquinoline (pq) 3; dppz = dipyrido[3,2-a:2',3'-c]phenazine) and their interaction with AAF adducted NarI DNA. Remarkably, complexes 1 and 2 displayed dominant 3LC transition characteristic of polar environment despite binding to the adducted sites. On the other hand, complex 3 binds to NarI sequences and behaves as a luminescent reporter for AAF-modified DNA. The results reported here emphasize that molecular light switching phenomenon can be stimulated by switching ancillary ligands and might act as potential probes for covalent-DNA defects.

The water soluble zinc based metal-organic frameworks (Zn-MOFs) as potential inhibitors for collagen fibrillogenesis.

Small molecules ranging from organic to inorganic systems have been reported as stabilizing agents for collagen. Various transition metal complexes have been utilized as tanning agent. However, as per the environmental norms issued by various regulatory agencies, the presence of certain metals such as Cr, Fe, Al, Zr and Ti in leather has been restricted to minimal amount (50 ppm), an unsurmountable task. To overcome the above issue and find an alternative tanning system, here in this study, we have reported the interaction of two water-soluble zinc-based metal-organic frameworks (MOFs), i.e., ZnPV (1) and ZnPA (2), with collagen using various spectroscopic techniques. Fibrillation kinetics studies showed that a significant delay in fibril formation with Zn-MOFs treated collagen was observed compared to the collagen untreated/ treated with individual ligands and metal salt. Circular dichroism studies show that at a low weight ratio (1:0.2 and 1:1::Collagen: MOF), no perturbation in the triple helical structure was observed, while at higher weight ratio (1:4), denaturation of collagen occurs. FT-IR studies showed that no perturbation was observed in the amide backbone in MOF-treated collagen. Differential scanning calorimetric data revealed that both Zn-MOFs increased the thermal denaturation temperature by 22 ± 2 °C compared to the collagen treated with individual entities. The viscosity of collagen rises with the increase in the concentration of Zn-MOFs. To the best of our knowledge, this is the first report on the use of the metal-organic framework as a stabilizing agent for collagen structure and might help in exploring the MOFs as potential tanning agents.

Structural insights into the recognition of DNA defects by small molecules.

Studies on the binding interaction of small molecules and nucleic acids have been explored for their biological applications. With excellent photophysical/chemical properties, numerous metal complexes have been studied as structural probes for nucleic acids. The recognition of DNA defects is of high importance due to their association with various types of cancers. Small molecules that target DNA defects in a specific and selective manner offer a new avenue for developing novel drugs and diagnostic tools. Transition metal complexes have been studied as probes for abasic sites and DNA/RNA mismatches. By changing the ligand structure or metal center, the probing efficiency of the metal complexes varies towards the defects. In this perspective, we have discussed mainly the structural requirement of metal complexes as probes for abasic sites, mismatches, and covalent DNA adducts, followed by the challenges and future directions.

Plasticity or elasticity? Relating elastic moduli with secondary structural features of mixed films of polypeptides at air/fluid and fluid/solid interfaces.

Viscoelastic properties of molecular assemblies formed by mixing poly (l-lysine) (PLL) and poly (l-glutamic acid) (PGA) at pH = 7.5 have been studied using Quartz crystal microbalance with dissipation (QCM-D). The inter-molecular complex between PLL and PGA arising from strong electrostatic interaction, leads to local changes in secondary structure resulting in intra-molecular complexes. ATR-FTIR analysis of the Secondary structural features of PLL, suggest an abundance of anti-parallel beta sheet that causes a significant change in the morphology of the self-assembled structures. A combination of spectroscopy, Brewster angle microscopy (BAM), Transmission electron and scanning electron microscopy show that an inverse relationship exists between the elasticity of the different PLL + PGA mixed films and the % anti parallel beta sheet conformation. The elastic moduli for the mixtures change from about 0.913 ± 0.01 GPa for pure PLL to about 0.764 ± 0.01 GPa in the mixture when PGA increases. The localized breaking and reformation of the ion pairs in the complex control their sizes and show an inverse relationship with the elastic moduli. The rheological profiles of the films, elastic moduli, together with their surface morphology from microscopy (TEM) and (SEM) confirmed their increasing propensity to self-assemble in one dimension to form tapes, colloidal particles and their composite assemblies.

Elastic compliance as a tool to understand Hofmeister ion specific effect in DMPC liposomes.

Elastic compliance of DMPC liposomes with Hofmeister electrolytes: NaCl, Na2SO4, Na2CO3, NaNO3, KCl and MgCl2 studied using Quartz crystal microbalance with dissipation has been correlated with changes in their lamellar spacing from SAXS. The study suggests that hydration water of the different ions has an effect on the overall packing of the lipid bilayer that results as either a dehydrated liposome or where water smears the surface of the liposomes. Ratio of hydrogen bonded carbonyl and phosphate of polar region of the liposomes from ATR-FTIR spectroscopy, suggests that the polar groups are less hydrated due to the displacement of water by the electrolytes compared to pure DMPC and ordered in the sequence for cations as: K+ < Na+,Mg2+ and for anions as SO42- < CO32- < Cl- < NO3-. These findings show the usefulness of Elastic compliance for structural studies of composite phospholipid bilayers, lipid-protein complexes and lipid systems of reduced dimensionalities.

Effect of chromium(III) gallate complex on stabilization of collagen.

To improve the stability of the collagen, here we studied the interaction of chromium(III) polyphenolic complex, [Cr(GA)2] (GA: Gallic acid) with collagen using various spectroscopic techniques. Circular dichroism studies show that the [Cr(GA)2] and gallic acid did not induce any structural perturbations on the triple helix of the collagen. Both differential scanning calorimetric(DSC) data and micro-shrinkage temperature studies showed that [Cr(GA)2] stabilized the collagen by 6±1°C compared to gallic acid. Hydrodynamic studies revealed that the viscosity of collagen drastically reduced in the presence of [Cr(GA)2] while gallic acid did not. Fibrillation assay displayed a significant delay in fibril formation with Cr(III) complex compared to gallic acid treated collagen. The inhibition of fibril formation was further confirmed by microscopic data in which collagen fibres are seen with GA while [Cr(GA)2] treated collagen exhibit a thin microfibrils. From AFM studies, the d-periodicity of collagen was found to be decreased with [Cr(GA)2] while increased with gallic acid. The present study deliberate the advantage of metal complex containing polyphenolic ligand as crosslinking agent due to its synergistic effect of both metal center as well as polyphenolic groups in the stabilization of collagen structure.

Interactions of Ru(II) polypyridyl complexes with DNA mismatches and abasic sites.

Polypyridyl based ruthenium(II) complexes, [Ru(bpy)2(furphen)](PF6)2 (1) and [Ru(bpy)2(imiphen)](PF6)2 (2) {furphen: 2-(furan-2-yl)-1H-imidazo[4,5-f][1,10]phenanthroline and imiphen: 2-(1H-imidazol-2-yl)-1H-imidazo[4,5-f][1,10]phenanthroline} were synthesized and characterized by ESI-MS, NMR, UV-Visible and fluorescence spectroscopic techniques. The interaction of Ru(II) complexes with calf-thymus DNA (CT DNA) as well as oligonucleotides containing mismatches and abasic sites was studied along with unmodified control DNA. Based on absorption titration studies, binding constants (Kb) for the interaction of complexes 1 and 2 with DNA were found to be 6.7 ± 0.2 × 10(3) and 4.9 ± 0.2 × 10(4) M(-1), respectively. Hydrodynamic studies revealed weak interactions between the two complexes and CT-DNA. Luminescence studies revealed that both the complexes exhibit a five-fold increase in emission upon addition of CT-DNA. The integrated emission intensity of complexes 1 and 2 with CC mismatch oligonucleotides was 1.5 and 1.2 fold higher than that of control GC match oligonucleotides, respectively. Both the complexes did not show any specificity towards abasic or other mismatch sites except for CC mismatch. The results from this study provide an insight into the requirements of ligand shape in recognising DNA mutations such as mismatch and selectivity between DNA mismatches.

Real-time surface plasmon resonance study of biomolecular interactions between polymerase and bulky mutagenic DNA lesions.

Surface plasmon resonance (SPR) was used to measure polymerase-binding interactions of the bulky mutagenic DNA lesions N-(2'-deoxyguanosin-8-yl)-4'-fluoro-4-aminobiphenyl (FABP) or N-(2'-deoxyguanosin-8-yl)-7-fluoro-2-acetylaminofluorene (FAAF) in the context of two unique 5'-flanking bases (CG*A and TG*A). The enzymes used were exo-nuclease-deficient Klenow fragment (Kf-exo(-)) or polymerase ß (pol ß). Specific binary and ternary DNA binding affinities of the enzymes were characterized at subnanomolar concentrations. The SPR results showed that Kf-exo(-) binds strongly to a double strand/single strand template/primer junction, whereas pol ß binds preferentially to double-stranded DNA having a one-nucleotide gap. Both enzymes exhibited tight binding to native DNA, with high nucleotide selectivity, where the KD values for each base pair increased in the order dCTP ≪ dTTP ∼ dATP ≪ dGTP. In contrast to that for pol ß, Kf-exo(-) binds tightly to lesion-modified templates; however, both polymerases exhibited minimal nucleotide selectivity toward adducted DNA. Primer steady-state kinetics and (19)F NMR results support the SPR data. The relative insertion efficiency fins of dCTP opposite FABP was significantly higher in the TG*A sequence compared to that in CG*A. Although Kf-exo(-) was not sensitive to the presence of a DNA lesion, FAAF-induced conformational heterogeneity perturbed the active site of pol ß, weakening the enzyme's ability to bind to FAAF adducts compared to FABP adducts. The present study demonstrates the effectiveness of SPR for elucidating how lesion-induced conformational heterogeneity affects the binding capability of polymerases and ultimately the nucleotide insertion efficiency.

Inhibitory effects of polyphenol punicalagin on type-II collagen degradation in vitro and inflammation in vivo.

Cartilage destruction is a crucial process in arthritis and is characterized by the degradation of cartilage proteins, proteoglycans, and type II collagen (CII), which are embedded within the extracellular matrix. While proteoglycan loss can be reversed, the degradation of CII is irreversible and has been correlated with an over-expression and over-activation of matrix metalloproteinases (MMPs). Among the various MMPs, the collagenase MMP-13 possesses the greatest catalytic activity for CII degradation. Here we show that the pomegranate-derived polyphenols, punicalagin (PA) and ellagic acid (EA), inhibit MMP-13-mediated degradation of CII in vitro. Surface plasmon resonance studies and molecular docking simulations suggested multiple binding interactions of PA and EA with CII. The effects of PA on bovine cartilage degradation (stimulated with IL-1ß) were investigated by assaying proteoglycan and CII release into cartilage culture media. PA inhibited the degradation of both proteins in a concentration-dependent manner. Finally, the anti-inflammatory effects of PA (daily IP delivery at 10 and 50mg/kg for 14days) were tested in an adjuvant-induced arthritis rat model. Disease development was assessed by daily measurements of body weight and paw volume (using the water displacement method). PA had no effect on disease development at the lower dose but inhibited paw volume (P<0.05) at the higher dose.

Importance of ligand structure in DNA/protein binding, mutagenicity, excision repair and nutritional aspects of chromium(III) complexes.

Chromium is extensively used in leather, chrome plating and refining industries. On one hand the occupational exposure to chromium leads to cancer, whereas on the contrary certain Cr(III) compounds have been proposed as nutritional supplements for Type II diabetes and as muscle building agents. Despite the positive outlook of chromium as a bio-essential element, there is increasing concern over the therapeutic application of Cr(III) based supplements, its bioavailability and toxicity profile. In this perspective, we discuss the role of ligand structure in mediating the interaction of chromium(III) complexes with DNA/protein, their mutagenic outcomes, adduct reparability and as nutritional supplements.

Binary and ternary binding affinities between exonuclease-deficient Klenow fragment (Kf-exo(-)) and various arylamine DNA lesions characterized by surface plasmon resonance.

We used surface plasmon resonance (SPR) to characterize the binding interactions between the exonulease-free Klenow fragment (Kf-exo(-)) and unmodified and modified dG adducts derived from arylamine carcinogens: fluorinated 2-aminofluorene (FAF), 2-acetylaminofluorene (FAAF), and 4-aminobiphenyl (FABP). Tight polymerase binding was detected with unmodified dG and the correct dCTP. The discrimination of correct versus incorrect nucleotides was pronounced with K(D) values in the order of dCTP ≪ dTTP < dATP < dGTP. In contrast, minimal selectivity was observed for the modified templates with Kf-exo(-) binding tighter to the FAAF (k(off): 0.02 s(-1)) and FABP (k(off): 0.01 s(-1)) lesions than to FAF (k(off): 0.04 s(-1)).

Sequence effects on translesion synthesis of an aminofluorene-DNA adduct: conformational, thermodynamic, and primer extension kinetic studies.

The DNA sequence effect is an important structural factor for determining the extent and nature of carcinogen-induced mutational and repair outcomes. In this study, we used two 16-mer template sequences, TG*A [d(5'-CTTCTTG*ACCTCATTC-3')] and CG*A [d(5'-CTTCTCG*ACCTCATTC-3')], to study the impact of the 5'-flanking nucleotide (T vs C) on aminofluorene (AF)-induced stacked (S)/major groove (B)/wedge (W) conformational heterogeneity during a simulated translesion synthesis. In addition, we probed the sequence effect on nucleotide insertion efficiencies catalyzed by the Klenow fragment (exonuclease-deficient) of DNA polymerase I. Our (19)F NMR/ICD/DSC results showed that AF in the CG*A duplex sequence adopts a greater population of S-conformer than the TG*A sequence. We found that the S conformer of CG*A thermodynamically favors insertion of A over C at the lesion site (n). Significant stalling occurred at both the prelesion (n - 1) and lesion (n) sites; however, the effect was more persistent for the S conformer of CG*A than TG*A at the lesion site (n). Kinetics show that relative nucleotide insertion frequencies (f(ins)) were greater for TG*A than the S conformer of CG*A for either dCTP or dATP at the lesion site (n), and the insertion rate was significantly reduced at immediate upstream base pairs (n, n + 1). Taken together, the results provide insight into how the mutagenic AF could exhibit an S/B/W equilibrium in the active site of a polymerase, causing different mutations. This work represents a novel structure-function relationship in which adduct structure is directly linked to nucleotide insertion efficiency in a conformation-specific manner during translesion DNA synthesis.

Investigating the biochemical impact of DNA damage with structure-based probes: abasic sites, photodimers, alkylation adducts, and oxidative lesions.

DNA sustains a wide variety of damage, such as the formation of abasic sites, pyrimidine dimers, alkylation adducts, or oxidative lesions, upon exposure to UV radiation, alkylating agents, or oxidative conditions. Since these forms of damage may be acutely toxic or mutagenic and potentially carcinogenic, it is of interest to gain insight into how their structures impact biochemical processing of DNA, such as synthesis, transcription, and repair. Lesion-specific molecular probes have been used to study polymerase-mediated translesion DNA synthesis of abasic sites and TT dimers, while other probes have been developed for specifically investigating the alkylation adduct O(6)-Bn-G and the oxidative lesion 8-oxo-G. In this review, recent examples of lesion-specific molecular probes are surveyed; their specificities of incorporation opposite target lesions compared to unmodified nucleotides are discussed, and limitations of their applications under physiologically relevant conditions are assessed.

Nucleobase-dependent reactivity of a quinone metabolite of pentachlorophenol.

Pentachlorophenol (PCP) is a possible human carcinogen detected widely in the environment. A quinone metabolite of PCP, tetrachloro-1,4-benzoquinone (Cl4BQ), is a reactive electrophile with the capacity to damage DNA by forming bulky covalent DNA adducts. These quinone adducts may contribute to chlorophenol carcinogenesis, but their structures, occurrence, and biological consequences are not known. Previous studies have indicated that several DNA adducts are formed in vivo in rats exposed to Cl4BQ, but these adducts were not identified structurally. In the present study, we have elucidated the structure of new agent-specific DNA adducts resulting from the reaction of dGuo, dCyd, and Thd with Cl4BQ. These have been characterized chemically by liquid chromatography-electrospray ionization mass spectrometry, HPLC, UV, and NMR analysis. Two dGuo adducts and one dCyd adduct resulting from the reaction of double-stranded DNA with Cl4BQ have been identified. The results indicate that, in the structural context of DNA, Cl4BQ reacts most readily with dGuo compared to the other DNA bases and that the mode of Cl4BQ reactivity is dependent on the base structure; i.e., multiple types of adducts are formed. Finally, DNA adducts consistent with Cl4BQ reactions are observed when DNA or dGuo is treated with PCP and a peroxidase-based bioactivating system.

Depurinating acylfulvene-DNA adducts: characterizing cellular chemical reactions of a selective antitumor agent.

Acylfulvenes (AFs) are a class of semisynthetic agents with high toxicity toward certain tumor cells, and for one analogue, hydroxymethylacylfulvene (HMAF), clinical trials are in progress. DNA alkylation by AFs, mediated by bioreductive activation, is believed to contribute to cytotoxicity, but the structures and chemical properties of corresponding DNA adducts are unknown. This study provides the first structural characterization of AF-specific DNA adducts. In the presence of a reductive enzyme, alkenal/one oxidoreductase (AOR), AF selectively alkylates dAdo and dGuo in reactions with a monomeric nucleoside, as well as in reactions with naked or cellular DNA, with 3-alkyl-dAdo as the apparently most abundant AF-DNA adduct. Characterization of this adduct was facilitated by independent chemical synthesis of the corresponding 3-alkyl-Ade adduct. In addition, in naked or cellular DNA, evidence was obtained for the formation of an additional type of adduct resulting from direct conjugate addition of Ade to AF followed by hydrolytic cyclopropane ring-opening, indicating the potential for a competing reaction pathway involving direct DNA alkylation. The major AF-dAdo and AF-dGuo adducts are unstable under physiologically relevant conditions and depurinate to release an alkylated nucleobase in a process that has a half-life of 8.5 h for 3-alkyladenine and less than approximately 2 h for dGuo adducts. DNA alkylation further leads to single-stranded DNA cleavage, occurring exclusively at dGuo and dAdo sites, in a nonsequence-specific manner. In AF-treated cells that were transfected with either AOR or control vectors, the DNA adducts identified match those from in vitro studies. Moreover, a positive correlation was observed between DNA adduct levels and cell sensitivity to AF. The potential contributing roles of AOR-mediated bioactivation and adduct stability to the cytotoxicity of AF are discussed.

Synthesis, characterization and DNA binding studies of two mixed ligand complexes of ruthenium(II).

Two mixed ligand complexes [Ru(bpy)(2)(DMHBT)]Cl(2)(1) and [Ru(phen)(2)(DMHBT)]Cl(2) (2) (where DMHBT is 11,13-dimethyl-13H-4,5,9,11,14-hexaaza-benzo[b]triphenylene-10,12-dione) have been synthesized and characterized by electrospray ionization (ESI) mass, (1)H-(1)H correlation spectroscopy (COSY), electronic spectroscopy, fluorescence spectroscopy and cyclic voltammetry. Spectroscopic titration and viscosity changes of calf thymus (CT)-DNA in the presence of incremental amount of complexes 1 and 2 clearly demonstrate that both these complexes bind intercalatively to DNA, with binding constant 2.87+/-0.20 x 10(4)M(-1) and 1.01+/-0.20 x 10(5)M(-1) for complexes 1 and 2, respectively. All the experimental evidences suggest that the ancillary ligand 2,2'-bipyridine (bpy) and 1,10-phenanthroline (phen) influences the intercalative binding of these complexes to DNA.

Characterization and biological activities of two copper(II) complexes with diethylenetriamine and 2,2'-bipyridine or 1,10-phenanthroline as ligands.

Two new mixed ligand copper(II) complexes with diethylenetriamine, 2,2'-bipyridine and 1,10-phenanthroline have been synthesized. The crystal and molecular structures of [Cu(dien)(phen)](ClO(4))(2) and [Cu(dien)(bipy)](BF(4))(2) (dien=diethylenetriamine, phen=1,10-phenanthroline, bipy=2,2'-bipyridine) were determined by X-ray crystallography from single crystal data. These two complexes have similar structures. The EPR spectral data also suggest that these complexes have distorted square pyramidal geometry about copper(II). Anti-microbial and superoxide dismutase activities of these complexes have also been measured. They show the higher SOD activity than the corresponding simple Cu(II)-dien/Cu(II)-PMDT (PMDT=N,N,N',N',N''-pentamethyldiethylenetriamine) complexes because of a strong axial bond of one of the nitrogen atoms of the alpha-diimine. Both the complexes have been found to cleave plasmid DNA in the presence of co-reductants such as ascorbic acid and glutathione.