Biology subjects

Zumrutdal, E.

Publications and source records attributed to Zumrutdal, E..

4 recordsLinked to original sources

bioRxiv2022

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. pIgs 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. Graphical abstractGraphic with abstract of the study. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=113 SRC="FIGDIR/small/516299v1_ufig1.gif" ALT="Figure 1"> View larger version (45K): org.highwire.dtl.DTLVardef@12ed4f6org.highwire.dtl.DTLVardef@19f7bb3org.highwire.dtl.DTLVardef@1726326org.highwire.dtl.DTLVardef@cb7f9d_HPS_FORMAT_FIGEXP M_FIG C_FIG

immunology↗

bioRxiv2022

Adsorption Race Between Activated Carbon and Lactase for Intermolecular Interaction with Lactose

BackgroundDisturbing dyspeptic complaints may be seen in the use of milk and dairy products in people with lactose intolerance. Lactose-free milk and dairy products are produced for people with these complaints. The widespread use of activated carbon for dyspeptic complaints can also be used for adsorbing lactose. MethodsFor this purpose, the binding energy of lactase to lactose was studied in silico, lactose adsorption enthalpic changes of activated carbon were calculated by HPLC, plain and activated carbon yoghurt was produced and glucose+galactose and lactose levels were determined in yoghurts. The effects of these yogurts on serum glucose levels were compared in mice. ResultsIn silico studies, the affinity of lactase with lactose was found to be -7.12 kcal/mol. It was determined by HPLC that activated carbon adsorbed lactose with an energy of -1,785 kcal/mol, and glucose+galactose levels and lactose ratios were lower in yogurt with added activated carbon. It was determined that there was no change in serum glucose levels in the 45th and 90th minutes following fasting in the mice fed with activated carbon yogurt compared to the mice fed plain yogurt. ConclusionYogurt with activated carbon can be an alternative diet for individuals with lactose intolerance, by converting lactose to lactase in the presence of lactase and adsorbing lactose in the absence of lactose.

bioengineering↗

bioRxiv2022

Virucidal Activity of Potassium Hydroxide Modeling on Tospovirus

Viral agents that cause disease in the respiratory system have led to widespread health problems in the world. The continuation of mutations in these viruses and the lack of an effective treatment agent bring possible public health risks. In this study, the virucidal activity of potassium hydroxide (KOH) was evaluated. The intermolecular interactions of KOH and envelope-structured molecules in enveloped viruses and the virucidal activity of these interactions on Tospovirus, which has the ability to infect, were evaluated. For this study model, the intermolecular interactions of KOH in the lipid bilayer of the virus envelope were evaluated in silico by Doking method. Then, the plant virulence ability of Tospovirus was observed by the direct interaction of KOH with Tospovirus. It was observed that KOH interacted exergonically with the glycerophosphate structure in the envelope structure. It was determined by clinical and laboratory observations that Tospovirus in plants lost its virucidal activity after interaction with KOH. In the light of this information, it was thought that KOH had a virucidal effect in enveloped viruses. It is thought that KOH creates this virucidal activity by KOH-glycerophosphate intermolecular interactions and viral envelope lipid layer hydrolysis. The mucolytic, alkalinizing and possible low-weight immunoglobulin-forming potential of KOH has been demonstrated in previous studies and no pathology was detected in toxicity studies in mice. In the light of this information, optimized KOH inhalation has a very serious potential as a virucidal agent in diseases caused by enveloped viruses in the respiratory system such as Coronavirus, H. influenza.

microbiology↗

bioRxiv2022

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

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.

immunology↗