Green Ionic Liquid Albumin Glassy Carbon Biosensor (ILAGC) for On-line Binding Studies of Human Serum Albumin with Retinol
- *Corresponding Author:
- Deia Abd El-Hady
Department of Chemistry
Faculty of Science-North Jeddah
King Abdulaziz University, Saudi Arabia
Received date: February 22, 2013; Accepted date: March 24, 2013; Published date: March 26, 2013
Citation: El-Hady DA, Albishri HM (2013) Green Ionic Liquid Albumin Glassy Carbon Biosensor (ILAGC) for On-line Binding Studies of Human Serum Albumin with Retinol. J Anal Bioanal Tech S7:004. doi: 10.4172/2155-9872.S7-004
Copyright: © 2013 El-Hady DA, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
A new biosensor composed of 1-butyl-3-methylimidazolium hexafluorophosphates (BMIMPF6)-human serum albumin (HSA) film coated on glassy carbon electrode (GCE) was produced. In the current work, the conjugation of ionic liquid (IL) with HSA improved the stability and binding affinity of protein onto GCE. A rapid and reliable voltammetric method for the on-line protein binding studies of retinol with HSA was developed by hyphenating ionic liquid albumin glassy carbon (ILAGC) biosensor with differential pulse anodic stripping voltammetry under physiological conditions. Detection limit and quantitation limit of 4.5 and 15.0 nmol L-1 were achieved, respectively. This gave us the opportunity to study the high binding constant between retinol and HSA by their detection in nanomolars. The electrochemical behavior of retinol onto ILAGC biosensor was monitored by cyclic voltammetry. The surface coverage of retinol on the proposed biosensor was calculated by double potential-step chronocoulometry. The binding constant of retinol with HSA was estimated to be 1.30×105 L mol-1 giving acceptable precision (SD ≤ 0.02) and good agreement with literature values. The proposed electrochemical biosensor opened a new venue for cheap, green and rapid on-line binding studies of small molecules with protein. As well, our proposed method could use to study either high or low binding affinities.