In order to study the wide scope of structural information of biomolecules in the presence of biocompatible cold atmospheric pressure plasma jets (CAPJ), we used circular dichroism (CD) and fluorescence experiments. Biomolecules are very sensitive and are highly complex systems, exhibiting a substantial degree of structural variability in their folded state. In the present investigation, we compared the compatiblity of α-chymotrypsin (CT) in the presence of biocompatible CAPJ. Using circular dichroism (CD) and fluorescence experiments, we describe the associated structural changes in CT after a 5 min treatment with CAPJ. The modifications in the secondary structure of this β/β protein were quantified by using the CD spectra. A reasonable decrease was observed for β-strands after treatment with CAPJ as compared to buffer, which contributes to its deterioration power. The implications of our results from studies delineating the effects of CAPJ on enzyme solutions are discussed.
All Science Journal Classification (ASJC) codes
- Physics and Astronomy(all)