6533b861fe1ef96bd12c5669
RESEARCH PRODUCT
Photoinduced and Self‐Activated Nuclease Activity of Copper(II) Complexes with N ‐(Quinolin‐8‐yl)quinolin‐8‐sulfonamide – DNA and Bovine Serum Albumin Binding
Francisco EstevanTamara TopalaGloria Alzuet-piñaAlejandro Pascual-álvarezFrancisca Sanzsubject
chemistry.chemical_classificationNucleasebiology010405 organic chemistryStereochemistryPhenanthrolineQuinolineIntercalation (chemistry)Plasma protein binding010402 general chemistry01 natural sciencesMedicinal chemistry0104 chemical sciencesSulfonamideInorganic Chemistrychemistry.chemical_compoundchemistrybiology.proteinBovine serum albuminDNAdescription
Two CuII complexes with a new quinoline sulfonamide derivative and phenanthroline (phen), [Cu(QSQ)(phen)]ClO4·0.5H2O (1) and [Cu(QSQ)(phen)(H2O)]ClO4 (2) [HQSQ = N-(quinolin-8-yl)quinolin-8-sulfonamide], have been synthesized and physicochemically characterized. Single-crystal X-ray diffraction studies have revealed a highly distorted trigonal-bipyramidal structure for 1 (τ = 0.68) and an almost perfect trigonal-bipyramidal geometry for 2 (τ = 0.92). DNA binding studies, which were performed by thermal denaturation, viscometry, fluorescence spectroscopy, and cyclic voltammetry, indicated a partial intercalation of 1 with Kapp = 2.45 × 106 M–1. The nuclease activity of 1 was investigated upon photoirradiation, with ascorbate/H2O2 as the activating agent, and also in the absence of any external reagent. In all cases, 1 was able to perform DNA cleavage, and its nuclease efficiency varied in the order ascorbate/H2O2 > photoirradiation > without external cofactors. Mechanistic investigations suggest an oxidative cleavage of DNA involving reactive oxygen species (ROS). The protein binding ability of 1 was also studied with bovine serum albumin (BSA) as a model protein.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2016-02-04 | European Journal of Inorganic Chemistry |