For an early and strong immune response in the monomerization of polymeric immunoglobulins intermonomeric interaction relationship of potassium hydroxide

Immunoglobulins (Ig), which are an integral part of the immune system in humans and animals, continue to surprise people with their effectiveness and importance every day since they were discovered for 2 centuries. Although the avidity of polymeric immunoglobulins (pIg) in the lumen in the respiratory system is high, its mobility is limited and unlike monomeric immunoglobulins (Ig), it can carry the antigenic (Ag) structure to the lamina propria by active transport. pIg's have a high weight because they have a large number of monomers. Disulfide bonds are important in the bonds that connect Ig monomers, and disulfide bonds have critical functions in construction, both in the J chain and in the intermonomeric domain. Disulfide bonds can interact quite easily with hydroxyl(OH-) ions. It is a strong molecular structure that gives OH- ions in potassium hydroxide (KOH). In our study, the potential of pIg to be made monomeric was investigated in order to increase the mobilization, antigen affinity and antigen avidity of pIgs (IgM and IgA) in the secretion in the lumen. For this purpose, intermonomeric disulfide bonds were determined by investigating cysteine locations in the J chain and on the monomers. In this study, by targeting these disulfide bonds, the intermolecular interaction energies with KOH for the destruction of these bonds were evaluated by in silico studies. Exergonic intermolecular free energy interactions were detected between the disulfide bonds in the J chain and in the intermonomeric domain and the KOH molecule.