Characterization of protein alterations in damaged axons in the brainstem following traumatic brain injury using fourier transform infrared microspectroscopy: a preliminary study.

Axonal injury contributes greatly to neurological dysfunction following traumatic brain injury (TBI), but current histological diagnostic methods are limited in identifying the pathological profiles of injured axons and unable to provide an objective and accurate quantification. Fourier transform infrared microspectroscopy (FTIRM) has the ability to offer macromolecular bioinformatics of the tissues including biochemical composition and structure by calculating band absorption intensity. In this study, axonal injury in the brainstem of rats with traumatic brain injury at 72 h post-trauma, which was confirmed with beta-amyloid precursor protein (β-APP) immunostaining, was detected with FTIRM technique. The lower intensity of infrared absorbance under the amide I band corresponds strongly to the area of axonal injury, and further analysis of amide I band shows significant differences in protein conformation between injured and normal axons. The findings indicate that using FTIRM technique, the amide I band has potentials to be a infrared spectral marker of axonal injury.