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.

Ionic Liquid Surfactant Mediated Structural Transitions and Self-Assembly of Bovine Serum Albumin in Aqueous Media: Effect of Functionalization of Ionic Liquid Surfactants

“…During this self-assembly, it is be possible that some of the ILS-3 remains intact with the self-assembling ILS sheet structure). 39,45,46 Out of all these conformational variants, the presence of intermolecular β-sheet structure also termed as anti-parallel β-sheet structure is a unique feature of amyloid structures. Figure 6 shows the second derivative FTIR spectral change of BSA in the presence of different amounts of ILS-3, where contrastingly different self-assembled long and helically twisted fibers have been observed.…”

Adsorption of bovine serum albumin on silicon dioxide nanoparticles: Impact of pH on nanoparticle–protein interactions

“…37,40 Previous studies of BSA adsorption have focused primarily on secondary structure analysis rather than protein surface coverage. 13,31,33,51,52 In this study, we combine ATR-FTIR spectroscopy and TGA to obtain the time-and pH-dependent spectra of BSA on SiO 2 and quantify the adsorption and the structure of BSA on the surface. Protein adsorption, protein coverage, and protein structure have not been investigated previously in an integrated study.…”

Identification of Skin Electrical Injury Using Infrared Imaging: A Possible Complementary Tool for Histological Examination

“…Consistent with the second derivative spectra, this loading plot shows that the discriminating negatively correlated loadings were found for normal epidermis at 1650 and 1697 cm -1 whereas positive loadings representative for electrical injury were present at 1621 and 1678 cm -1 . The observed spectral pattern is similar to those of bovine serum albumin (BSA) with increasing temperatures, which reveals that gradually decreased α-helix content with predominance of β-sheet as the temperature increases [21]. Therefore, this result may be associated with protein denaturation caused by Joule heating.…”