Published May 2015 | Version v1
Journal article

A control on hydrophobic and hydrophilic interactions between HEWL and metal Schiff-base complexes comprising of different metal ions and ligands

Description

The structural effects of different copper(II) and nickel(II) Schiff base complexes on hen egg white lysozyme (HEWL) have been investigated through steady state and time resolved absorption and fluorescence, and circular dichroism spectroscopy. The Schiff base ligands with N4 donor atoms show both hydrophobic and hydrophilic interactions, however hydrophilic interaction prevails with ligands having N2O2 donor atoms. Variation of metal ions from Cu2+ to Ni2+ with each type of Schiff base ligand increases the probability of hydrophilic over hydrophobic interactions, which supports their significance in regulating the binding affinity between HEWL and metal complexes. On photo-excitation the complexes comprising of Cu2+ ion instead of Ni2+ ion and ligands with N4 donor system rather than N2O2 donor system, increases the probability of intersystem crossing to populate the corresponding triplet state as observed from laser flash photolysis study. The better binding affinity of nickel complexes with different selectivities compared to copper complexes towards HEWL emphasizes the potentiality of less explored nickel complexes in drug–protein interactions. - Highlights: • NiII and CuII -Schiff base complexes bind hen egg white lysozyme spontaneously. • Both hydrophobic and hydrophilic interactions are effective for N4 ligands. • For N2O2 ligands the hydrophilic is predominant over hydrophobic interaction. • Binding affinity and selectivity of NiII-complexes are better than CuII-complexes. • Replacement of Cu2+ by Ni2+ in a ligand enhances chance of hydrophilic interaction

Availability note (English)

Available from http://dx.doi.org/10.1016/j.jlumin.2014.12.027

Additional details

Identifiers

DOI
10.1016/j.jlumin.2014.12.027;
PII
S0022-2313(14)00732-7;

Publishing Information

Journal Title
Journal of Luminescence
Journal Volume
161
Journal Page Range
p. 54-62
ISSN
0022-2313
CODEN
JLUMA8

Optional Information

Copyright
Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.