Issue 3, 2015

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Abstract

Attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy using a special waveguide based on a silver halide fiber was used for probing the heat-induced secondary structure and conformation changes of bovine serum albumin (BSA). From the secondary derivative and the curve fitting of the obtained ATR-FTIR spectra, the changes of the BSA secondary structure with temperature were clearly identified. Two different thermal denaturation temperature ranges (i.e., 50–52 and 80–82 °C, at which a change of the protein structure occurred) were determined, while only one denaturation temperature was previously identified via classical FTIR measurements. Additionally, taking advantage of two-dimensional correlation spectroscopy more detailed information on changes of the protein secondary structure was revealed. The developed method facilitates in situ, sensitive, and more in-depth probing of protein secondary structures, which represents a significant advancement compared to conventional characterization methods.

Graphical abstract: Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

Article information

Article type
Paper
Submitted
14 Aug 2014
Accepted
11 Nov 2014
First published
12 Nov 2014
This article is Open Access
Creative Commons BY license

Analyst, 2015,140, 765-770

Author version available

Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors

R. Lu, W. Li, A. Katzir, Y. Raichlin, H. Yu and B. Mizaikoff, Analyst, 2015, 140, 765 DOI: 10.1039/C4AN01495B

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