Affordable Access

Publisher Website

Voltammetric and spectroscopic studies on the interaction of tilmicosin with bovine serum albumin at different pHs

Authors
Journal
Journal of Electroanalytical Chemistry
1572-6657
Publisher
Elsevier
Publication Date
Volume
657
Identifiers
DOI: 10.1016/j.jelechem.2011.04.001
Keywords
  • Tilmicosin
  • Bovine Serum Albumin
  • Interaction
  • Voltammetry
  • Spectroscopy
Disciplines
  • Physics

Abstract

Abstract In this study, the voltammetric behavior of the interaction between tilmicosin (TIM) and bovine serum albumin (BSA) was investigated using voltammetry and UV–Vis spectroscopy techniques. In the presence of BSA, the main reductive signal of TIM gradually decreased without the appearance of new peaks. The formation of a 1:1 complex between TIM and BSA were determined at different pHs (3, 7.4 and 11). This interaction was also supported by ultraviolet spectroscopy. After the addition of TIM into the BSA solution, at pH 3 and 7.4, the absorption band of BSA at 217 nm decreased, shifted to smaller wavelengths, and narrowed. However, at pH 11, the absorbance of BSA at 217 nm decreased without the shift of maximum absorption wavelength. The interaction between TIM and BSA was mainly sourced from electrostatic or hydrophobic (intercalation) interactions.

There are no comments yet on this publication. Be the first to share your thoughts.