Physicochemical and Structural Characterisation of Human Il-1α and Il-2 Proteins with Insilco Tools

Abstract

Inflammation is a physiological reaction that occurs as a result of several types of injuries, including those caused by physical, chemical, or biological sources. Interleukins, which belong to the wider category of cytokines, modify cellular function in the context of inflammation. Interleukins are used in animal experiments to explore aspects linked to healthcare. The interleukin-1α and interleukin-2 families are particularly associated with harmful inflammatory processes, even more so than any other kind of cytokine. The objective of the current work was to analyze the physiochemical characteristics, secondary structures, and tertiary structures of IL-1α and IL-2 utilizing bioinformatic techniques. The amino acid sequences of IL-1α and IL-2 were obtained from the UniProt protein database. The physicochemical characterisation of IL-1α and IL-2 proteins showed that they are made up of 271 and 153 amino acids, with molecular weights of 30606.61 and 17627.1 Da, respectively. The predicted isoelectric (pI) values for the IL-1α and IL-2 peptides were determined to be 5.04 and 7.67, respectively. In their secondary structures, the IL-1α and IL-2 proteins display a higher proportion of extended strands and alpha helices respectively. The predicted 3D structure of IL-1α and IL-2 from humans demonstrates that P01583.1.A and P60568.1.A are the most appropriate templates. The QMEAN values for the predicted models of IL-1α and IL-2 were 0.51±0.05 and 0.73±0.07, respectively. The Ramachandran plot showed that most of the amino acid phi-psi distributions are in line with a right-handed helix. These results confirm that the expected model is stable and reliable.