To study the influence of electromagnetic fields on the vibration bands of bovine serum albumin linkages and to check the eventual bioprotective effectiveness of trehalose (a disaccharide) on the stability of the secondary structure of the protein.
Two samples of different bovine serum albumin aqueous solutions (100 mg/ml) were exposed (partly with 80 mg/ml trehalose) and measurements were performed after 2 h or 4 h of exposure.
Proteins exist in different structures (e.g. beta-sheet and alpha-helix structure are typical secondary protein structures) generating different vibration bands within the FTIR spectroscopy (an infrared spectroscopy). Different amide bands originating from vibrations of the peptide or protein backbone are characteristic for protein vibration spectra.
samples were exposed in eight groups: i) static magnetic field (SMF) + D2O ii) SMF + D2O-trehalose iii) 50 Hz magnetic field (AC) + D2O iv) AC + D2O-trehalose v) SMF + H2O vi) SMF + H2O-trehalose vii) AC + H2O viii) AC + H2O-trehalose
|Exposure duration||continuous for 2 h or 4 h|
|magnetic flux density||1.8 mT||maximum||measured||-||-|
|magnetic flux density||200 mT||-||measured||-||-|
An alteration of the secondary structure of bovine serum albumin, represented by a clear decrease in amide A and amide I vibration band intensities, was observed after exposures for up to 4 h to the static magnetic field and the extremely low frequency electromagnetic field of protein samples in H2O and D2O aqueous solutions, leading the authors to the assumption that a loss of C=O and C-N stretching vibrations and NH linkages occurred in the secondary structure of the protein.
By contrast, bovine serum albumin in trehalose aqueous solution was almost unchanged after the exposure to the static magnetic fields and extremely low frequency electromagnetic fields, supporting the hypothesis that trehalose can preserve the protein from electromagnetic fields.