SPE7 Synthesis

As Bayry et al explains in their journal article antibodies from healthy immune groups will somehow bind to heme and acquire the ability to recognize multiple antigens. It was originally thought that all antibodies bonded to their individual antigens in a lock and key sort of function. However, several similar studies, such as the experiment performed by Bayry et al, have led to a much different consensus. It has now been determined that many antibody molecules are capable of changing its conformation to allow for its flexible antigen-binding pocket to accommodate several different antigens to interact with the antibody. The following process is a basic process of how the body works to rid the body of foreign antigens. Whether the antibody …show more content…
It has also been shown that SPE7 is one of the several antibodies that are able to be polyreactive, resulting in bonding to several different antigens. In addition to this, SPE7 has also been shown to typically bind to other aromatic compounds with a high affinity as well3. When SPE7 undergoes promiscuous binding, it has been shown that there are two typical ways that it accomplishes this, induced fit and conformational isomerism3. Induced fit, much like the lock and key process discussed earlier occurs when an enzyme or an antibody binds to its appropriate substrate or antigen13. When this process occurs, the antibody will experience subtle changes in its active site to allow for the antigen to fit into the active site. This induced fit enhances the ability of the antibody to destroy the antigen, or allows for the enzyme to convert substrate to product in the scope of the enzyme and its substrate13. Release of the destroyed antigen restores the antibody to its original form which allows for the antibody to go around and find other antigens to destroy in a similar fashion as long as similar antigens are present. Conformational isomerism, on the other hand, is when stereoisomers are converted into one another by rotation around a single bond14. SPE7 in its equilibrium state has been shown to exist in at least two conformational isomers, one less prevalent isomer that exhibits a deep and narrow binding site used to recognize smaller aromatic molecules and another more prevalent isomer with a wide and shallow binding site that enables the antibody to recognize several different protein antigens14. Due to this conformational isomerism phenomenon, the dynamics of this structure allows for SPE7 to bind to several different types of antigens16. In addition, the less prevalent isomer of SPE7 that utilizes induced-fit binding allows for several different antigens to be