BlOG

Представлены расчеты, методы подбора и даны характеристики ингибиторов образования высокомолекулярных структур амилоидными пептидами, дано объяснение их блокирующему действию. Подробно рассмотрены биофизические требования к ингибиторам, критерии и условия их отбора, которые будут блокировать образование амилоидами структур высокого порядка. В качестве ингибиторов были изучены модифицированные пептиды, которые будут образовывать с амилоидными пептидами устойчивые димеры

We have developed a unique innovative biophysical concept, as well as the corresponding software, which allows us to represent biology not only as an exclusively experimental section of the natural sciences, but also to study this section from the point of view of the exact sciences. Thus, it will allow studying biology from the point of view of exact sciences. Our main mission is to enable drug developers to use our innovative methodology to analyze the interactions of amino acid sequences before the experiment and then adjust the experimental problems.

Now we have an Instagram account, which presents short sentences and the results of our work. You can connect to our instagram account and follow the news from a convenient application from any device.
The main emphasis here is placed on a visually understandable presentation in the presentation of material in the form of posters and presentations

We have updated the main page, added a description of biophysical aspects in the field of determining the affinity of the antibody-antigen biocomplex. The correct determination of antibody affinity is crucial for antibody development as a wrong setup of the experiments may result in the further development of the wrong candidate antibody. This can result in low in vivo efficacy, especially when high-affinity antibodies are needed, for example, for neutralizing antibodies

This article describe a detailed method for selecting inhibitors based on modified natural peptides for the SARS-CoV protein spike glycoprotein. The selection of inhibitors is carried out by increasing the affinity of the peptide to the active center of the protein. The article also provides a step-by-step guide to the analysis of affinity of interaction by comparing 3 criteria, presents an analysis of energy interactions between the active center of a protein and the wild-type peptide interacting with it and taking into account modifications of the latter.

The most common explanation is that hydrophobic molecules "do not like" to interact with the aqueous environment. We obtained the values of hydrophobic interactions, calculated their value, developed a method for determining the range of interactions, and developed a graphical representation

The most common explanation is that hydrophobic molecules "do not like" to interact with the aqueous environment. We obtained the values of hydrophobic interactions, calculated their value, developed a method for determining the range of interactions, and developed a graphical representation

We have developed a technique for the formation of stable dimeric complexes involving amyloid peptides, which tend to form amyloid plaques. One of the mechanisms responsible for the formation of amyloid plaques is the introduction of amyloid peptides into biochemical reactions on the way to achieving chemical and thermodynamic equilibrium.