Interaction of the Zn2+ and Cu2+ complexes of terpyridine appended glucosyl-conjugate with wheat germ agglutinin and DNA. (1st November 2019)

• Record Type: Journal Article
• Authors: Dinda, Subrata Kumar; Upadhyay, Aekta; Hussain, Md. Althaf; Rao, Chebrolu Pulla
• Is Part Of: Polyhedron. Volume 172(2019)
• Page Start: 148
• Page End: 156
• Publication Date: 2019-11-01
• Subjects: Glucosyl derivative -- Terpyridyl binding core -- ct-DNA -- Wheat germ agglutinin -- Plasmid cleavage -- Dendrimeric-like protein aggregation; Chemistry, Inorganic -- Periodicals; Chimie inorganique -- Périodiques; Organometaalverbindingen; Anorganische chemie; 546.05
• DOI: 10.1016/j.poly.2019.04.014
• Languages: English
• ISSNs: 0277-5387

Abstract

Graphical abstract: The Zn 2+ and Cu 2+ complexes of glucosyl appended, triazole linked terpyridyl motif binds to biomolecules, such as, DNA and proteins and therefore, qualifies to be of biological importance. Abstract: The terpyridine appended glucosyl-conjugate ligand L and its complexes of Zn 2+ (1 ) and Cu 2+ (2 ) were synthesized and characterized by spectroscopy techniques. The changes in the absorption and fluorescence spectra of L in presence of Zn 2+ and Cu 2+ is supportive of interaction of L through terpyridyl metal binding core which was further confirmed by 1 H NMR. The coordination and structural features emerged from the spectroscopy were used in order to optimize the structures of 1 and 2 by DFT computational calculations. The isolated complex 2 shows binding with ct-DNA through minor groove binding and intercalation modes and increases the thermal stability of ct-DNA by ∼20 °C. Due to the presence of Cu 2+ in 2, this complex showed cleavage of the plasmid pBR322 through hydroxy radical formation. The presence of glucosyl moiety at both the ends of the complex 1 interacts with the WGA and imparts dendrimeric-like micro structures due to the protein aggregation as demonstrated by SEM.