Saponaria Officinalis

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Saporin S6 is a compound that was isolated from the Saponaria officinalis, a plant known as soapwart. It has been studied for almost thirty years due to its unique properties in medical science. It is a protein that has had many studies done testing its potential application towards anti-tumor and anti-viral therapy. This particular article describes the reasons for its high stability towards denaturing agents. Protein are susceptible to denaturalization under specific conditions like temperature or the chemical environment that it is in. A protein’s structure also contributes to its stability. Researchers are looking at all the properties of this specific protein that allows it to remain its folding structure and function under abnormal conditions. …show more content…

The active site of the protein is located at the cleft between the subdomains. It is characterized as a mix of type 1 and type 2 RIPs. Around the N-terminus, there are 6 β-sheets, 4 antiparallel strands and 2 parallel strands. The C-terminus has 8 α-helices where the 310-helix crosses over on the parallel β-strand giving a canonical geometry. Unlike RIPs, Saporin-S6 has 2 β-strands (7 & 8) that are shorter that increases the accessibility to a particular substrate. This plays a role with its resistance to denaturing agents, the ability to survive in extreme pH, the modifications that are necessary to create immunotoxin and the stability in extreme temperatures. Researchers used a Fourier transform infrared (FTIR) spectroscopy to observe the thermal stability of Saporin-S6 and induced the unfolding of the protein. The Fourier transform infrared spectroscopy provided information that was necessary to determine the correct structure. There was a table that listed the different peak values that represented the strength of the bonds between the atoms in the molecule. Based …show more content…

It was evident that the three dimensional structure of Saporin-S6 was highly occupied with α helices based on the percentage of the peak ratios. It is important to look at the intensity of the peak or broadness of the peak to identify the bonding strength of two molecules. By observing the peaks of the different bond possibilities, its structure can be determined. Once the structure is fully determined, peaks that would show a major change were chosen to observe how the structure of the protein changed. It is the disappearance of the peaks in a spectrum that would indicate the defolding of Saporin-S6. If there are new peaks that occur in the final results, it indicated the aggregation of the unbroken strands of the protein. Saporin-S6 is a protein that is made up of 253 amino acids. To simplify the data analysis, these scientist

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