The Interactions of Potassium Hydroxide in the Vicinity of Connective Disulfide Bonds of the Fab Regions of Some Human Immunoglubulins: Preliminary Computational Implications for Affinity on Cys-Cys Disulfide Bridges

Abstract

The average human lifespan continues to increase with the increase in data flow and the advancement of related technological developments. However, this development brings with it many diseases, including immunological problems. Immunoglobulin varieties found in different organisms in the last 3-4 decades continue to be hope for many diseases. Interest has focused on the lesser weight but more mobile immunoglobulins found in camelids. Later, different types of these antibodies were tried to be made with biotechnological engineering and their effectiveness continues to be investigated. Disulfide bridges located on the immunoglobulin are one of the key points for the structure and function of the immunoglobulin. The interest of potassium hydroxide in disulfide bridges may enable us to damage or break these bonds. For this purpose, in this study, the relationship between disulfide bridges between light and heavy chains and potassium hydroxide was investigated. It was observed that the affinity of potassium hydroxide to disulfide bridges occurred exergonically. In the light of this information, it can be thought that lighter, more functional immunoglobulin fragments and nanobodies can be formed with potassium hydroxide compared to conventional immunoglobulin.

Virucidal Activity of Potassium Hydroxide Modeling on Tospovirus

“…In another study with the KOH molecule, the affinity of KOH for disulfide bonds in some human immunoglobulins (Ig) Fab region was demonstrated by intermolecular interactions (27). These findings suggest that KOH potentially induces low-weight Ig production.…”

"Short Communication on the Potential Activity of Potassium Hydroxide on the Formation of Low-Weight Immunoglobulin"

“…In this way, there have been developments in the treatment of many diseases such as allergic, immunological, viral diseases or cancer. In the in silico study included in the discussion, it was found that the binding affinity of KOH to the region of the disulfide bonds between the heavy and light chain on the Ig structure with -1 kcal/mol increased up to the level of -3 kcal/mol with the increase in the number of KOH molecules [3]. The study showed the potential of this effect to form new small-weight Ig by breaking the disulfide bond between the heavy and light chains (Figure 1).…”