Quantitation of Molecular Interactions Based on the Avidin-Biotin Complex by Dielectric Spectroscopy

Authors

Stephen Wood, Brigham Young University
Dr. Brian Mazzeo, Brigham Young University

Keywords

dielectric spectroscopy, avidin-biotin complex, agilent impedance analyzer

College

Ira A. Fulton College of Engineering and Technology

Department

Electrical and Computer Engineering

Abstract

The interaction of proteins with other molecules is a common phenomenon that is relevant to various disciplines such as medicine and material science. There are several aspects regarding these molecular interactions that can be researched with one of several measurement techniques. Dielectric spectroscopy is an inexpensive and non-invasive technique used to probe the electrical properties of materials. It was developed in the early twentieth century as a method to measure the change in the dielectric constant of a material in response to changes in frequency. The change or relaxation in the dielectric constant as a function of frequency allows for the calculation of the dipole moment and the effective radius of a large molecule or aggregate. In this study, dielectric spectroscopy was used to quantify the interaction of avidin and biotin. Biotin is a ligand that binds with avidin to form a structure. In theory, a titration experiment can be performed to determine the saturation limit of biotin that binds with a given amount of avidin.

Recommended Citation

Wood, Stephen and Mazzeo, Dr. Brian (2014) "Quantitation of Molecular Interactions Based on the Avidin-Biotin Complex by Dielectric Spectroscopy," Journal of Undergraduate Research: Vol. 2014: Iss. 1, Article 88.
Available at: https://scholarsarchive.byu.edu/jur/vol2014/iss1/88