Abstract

Equilibrium studies in aqueous solution are reported for dibutyltin(IV) (DBT) complexes of the zwitterionic buffers “Good’s buffers” Mes and Mops. Stoichiometric and formation constants of the complexes formed were determined at different temperatures and ionic strength 0.1 mol·L−1 NaNO3. The results show that the best fit of the titration curves were obtained when the complexes ML, MLH−1, MLH−2 and MLH−3 were considered beside the hydrolysis product of the dibutyltin(IV) cation. The thermodynamic parameters ΔH o, ΔS o and ΔG o calculated from the temperature dependence of the formation constant of the dibutyltin(IV) complexes with 2-(N-morpholino)ethanesulfonic acid (Mes) and 3-(N-mor-pholino)-propanesulfonic acid (Mops) were investigated. The effect of dioxane as a solvent on the formation constants of DBT–Mes and DBT–Mops complexes decrease linearly with the increase of dioxane proportion in the medium. The concentration distribution of the various complexes species was evaluated as a function of pH.

Highlights

  • Organotin(IV) compounds are receiving increasing interest because of their biological and potential pharmaceutical applications as antitumor agents [1,2,3,4,5,6]

  • The results show that the best fit of the titration curves were obtained when the complexes ML, MLH-1, MLH-2 and MLH-3 were considered beside the hydrolysis product of the dibutyltin(IV) cation

  • The thermodynamic parameters DHo, DSo and DGo calculated from the temperature dependence of the formation constant of the dibutyltin(IV) complexes with 2-(N-morpholino)ethanesulfonic acid (Mes) and 3-(Nmor-pholino)-propanesulfonic acid (Mops) were investigated

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Summary

Introduction

Organotin(IV) compounds are receiving increasing interest because of their biological and potential pharmaceutical applications as antitumor agents [1,2,3,4,5,6]. There has been an increase in reports on buffer interferences when most of Good’s buffers were used in the presence of metal ions [10,11,12,13,14,15,16]. Many conflicting data and conclusions that were reported by investigators studying identical metal cation protein systems (at the same pH in carefully executed experiments) might be due in part to the failure to include the presence of metal–buffer complexes

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