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Photoinduced and Self‐Activated Nuclease Activity of Copper(II) Complexes with N ‐(Quinolin‐8‐yl)quinolin‐8‐sulfonamide – DNA and Bovine Serum Albumin Binding
Author(s) -
PascualÁlvarez Alejandro,
Topala Tamara,
Estevan Francisco,
Sanz Francisca,
AlzuetPiña Gloria
Publication year - 2016
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201501469
Subject(s) - chemistry , bovine serum albumin , nuclease , intercalation (chemistry) , trigonal bipyramidal molecular geometry , dna , medicinal chemistry , stereochemistry , crystallography , crystal structure , inorganic chemistry , biochemistry
Two Cu II complexes with a new quinoline sulfonamide derivative and phenanthroline (phen), [Cu(QSQ)(phen)]ClO 4 · 0.5H 2 O ( 1 ) and [Cu(QSQ)(phen)(H 2 O)]ClO 4 ( 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 K app = 2.45 × 10 6 M –1 . The nuclease activity of 1 was investigated upon photoirradiation, with ascorbate/H 2 O 2 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/H 2 O 2 > 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.