examples
This section presents some examples of work.
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GET EXCLUSIVE RIGHTS TO AMYLOID PEPTIDE INHIBITORS
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.
At the moment, we have received a large amount of data on amyloid peptide inhibitors, we are conducting a fundraising company to conduct an experiment and create a database.
If you are interested in this topic, as well as the transfer of rights to the further use of the inhibitors found for scientific, practical, laboratory, pharmacological purposes, you can contact us and receive exclusive data with the transfer of use rights
At the moment, we have received a large amount of data on amyloid peptide inhibitors, we are conducting a fundraising company to conduct an experiment and create a database.
If you are interested in this topic, as well as the transfer of rights to the further use of the inhibitors found for scientific, practical, laboratory, pharmacological purposes, you can contact us and receive exclusive data with the transfer of use rights
INHIBITION OF AMYLOID PEPTIDES
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.
We propose a technique for achieving equilibrium at the level of dimeric complexes, so that amyloid peptides will form lower molecular weight complexes to a lesser extent.
The technique developed by us is in good agreement with previously performed experimental work, namely, we were able to determine the key amino acid residues that introduce the greatest instability in amyloid complexes. As criteria determining the stability and stability of the biochemical complex, in this case, we measure the change in the differential entropy of the complex, as well as the value of lg (cond (W)).
We propose a technique for achieving equilibrium at the level of dimeric complexes, so that amyloid peptides will form lower molecular weight complexes to a lesser extent.
The technique developed by us is in good agreement with previously performed experimental work, namely, we were able to determine the key amino acid residues that introduce the greatest instability in amyloid complexes. As criteria determining the stability and stability of the biochemical complex, in this case, we measure the change in the differential entropy of the complex, as well as the value of lg (cond (W)).
