Issue 9, 2012
From the journal:

Dalton Transactions

Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes†

Heather F. Crouse,a   Julianne Potoma,a   Farhat Nejrabi,b   Deanna L. Snyder,a   Balwant S. Chohanb  and  Swarna Basu*a  

* Corresponding authors

a Department of Chemistry, Susquehanna University, 514 University Avenue Selinsgrove, USA
E-mail: basu@susqu.edu
Fax: 1-570-372-2752
Tel: 1-570-372-4223

b Penn State Harrisburg, 777 West Harrisburg Pike, Middletown, PA 17057, USA

Abstract

A series of twelve anionic, cationic, and neutral nickel(II) complexes have been synthesized and characterized. The interaction of these complexes with bovine serum albumin (BSA), human serum albumin (HSA), lysozyme (Lyso), and tryptophan (Trp) has been studied using steady-state fluorescence spectroscopy. Dynamic and static quenching constants have been calculated, and the role played in quenching by the ligand and complex charge investigated. The nickel complexes showed selectivity towards the different proteins based on the environment surrounding the Trp residue(s). Only small neutral complexes with hydrophobic ligands effectively quenched protein fluorescence via static quenching, with association constants ranging from 102 M−1 (free Trp) to 1010 M−1 (lysozyme), indicating a spontaneous and thermodynamically favorable interaction. The number of binding sites, on average, was determined to be one in BSA, HSA and free Trp, and two in lysozyme.

Graphical abstract: Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes

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Article information

DOI
https://doi.org/10.1039/C2DT12169G
Article type
Paper
Submitted
13 Nov 2011
Accepted
22 Nov 2011
First published
16 Jan 2012

Dalton Trans., 2012,41, 2720-2731

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Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes

H. F. Crouse, J. Potoma, F. Nejrabi, D. L. Snyder, B. S. Chohan and S. Basu, Dalton Trans., 2012, 41, 2720 DOI: 10.1039/C2DT12169G

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