Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors. Issue 3 (19th December 2014)

• Record Type: Journal Article
• Authors: Lu, Rui; Li, Wen-Wei; Katzir, Abraham; Raichlin, Yosef; Yu, Han-Qing; Mizaikoff, Boris
• Is Part Of: Analyst. Volume 140:Issue 3(2015)
• Page Start: 765
• Page End: 770
• Publication Date: 2014-12-19
• Subjects: Chemistry, Analytic -- Periodicals; 543
• DOI: 10.1039/c4an01495b
• Languages: English
• ISSNs: 0003-2654

Abstract

Abstract : Planar silver halide fiberoptic sensors were used for the first time for studying the mechanism of heating induced bovine serum albumin (BSA) denaturation by deconvoluted infrared attenuated total reflection (IR-ATR) spectra, and two-dimensional correlation spectroscopy (2D-CoS). 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.