pH-dependent Structural Changes of Bovine Serum Albumin: Fluorescence and Circular Dichroism Spectroscopy Combined with Molecular Modeling

Abstract

Serum albumin is often used as a matrix for chemical and biomedical engineering, and therefore is a good model for studying their properties under non-physiological conditions. Imprinting of proteins is one such prominent example, due to the mounting awareness of the need to have robust approaches to produce biomimetic receptors. The structural complexity of the three-dimensional structure of an individual protein depends on the interaction of electrostatic, hydrophobic, hydrogen bonds and other interactions, modifications of which can lead to significant conformational changes. By altering the electrostatic charges on protein surfaces in a targeted manner, we can change the original protein structure, thereby affecting its original functions and bioavailability of protein-based systems.
In this work we used a broad array of quantitative techniques that yield a more exhaustive characterization of the structural changes of the bovine serum albumin induced by pH changes. We evaluate the secondary and tertiary structure of bovine serum albumin molecules at low pH value via fluorescence and circular dichroism spectroscopy. We also address whether modern, molecular modelling methods can sufficiently explain the mechanism behind the change of spectral signal.

Speaker

Polina M. Soboleva
Saratov State University
Russia

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