Oxidative stress induced conformational changes of human serum albumin.

Oxidative stress, generated by reactive oxygen species (ROS), is responsible for the loss of structure and functionality of proteins and is associated with several aging-related diseases. Here, we report an study to gauge the effect of ROS on the structural rearrangement of human serum albumin (HSA), a plasma protein, through metal-catalyzed oxidation (MCO) at physiological temperature through various biophysical techniques like UV-vis absorption, circular dichroism (CD), differential scanning calorimetry (DSC), MALDI-TOF, FTIR, and Raman spectroscopy. The UV-vis spectra of oxidized HSA show an early blueshift, signifying the unfolding of the protein because of ROS followed by the broadening of the absorption peak at a longer time.

Structural rearrangement of elastin under oxidative stress.

Reactive oxygen species (ROS) are key elements in several physiological processes. A high level of ROS leads to oxidative stress that damages biomolecules and is linked to many diseases like type-2 diabetes, cancer, inflammation, and many more. Here, our in-vitro study aimed to gauge the effect of ROS on the structural rearrangement of elastin through metal-catalyzed oxidation (MCO) at physiological temperature through laser light scattering, UV-vis, FTIR, and FESEM imaging.