German scientists successfully developed molecular light switch

German scientists have successfully developed a water-soluble light-sensitive polypeptide structure, whose biological functions can be controlled by light, and further research will be expected to achieve accurate delivery of cancer drugs. The relevant research results were published in the recently published Journal of Applied Chemistry.

Soluble substances such as drugs are usually distributed evenly in the body. Although some of them can reach their target areas, a large part of them are distributed to places where they do not want them to go. Therefore, scientists have been trying to develop a method to accurately control the time and space of drug action. For example, when a selected cell area (eg, a tumor area) is reached, the corresponding active substance is activated and leaves the area and loses its activity.

Now scientists from the Leibniz Institute for Molecular Pharmacology (FMP) and Berlin University of Technology have taken a crucial step in this direction and have successfully developed the first water-soluble light-sensitive polypeptide structure that can be biologically functional. Use light control. Scientists inserted optical switches in the polypeptide model, which is part of the bioactive protein model. When the switch is in the ground state, it blocks the binding of the polypeptide to the protein; after the switch is "switched" by light, it allows the polypeptide to bind to the target protein.

Polypeptides consist of amino acids in a sequence that exchanges biological information with other molecules, including proteins. Control of blood glucose levels in ***, as well as gastrin stimulate the formation of gastric acid contains peptides. Peptides have an influence on the specific functions of the body. In addition, they also have the advantage of being an endogenous substance, and they hardly trigger a defensive reaction. By connecting hydrogen bonds to each other, the polypeptide can change its shape. This so-called secondary structure has several forms such as α-helix and β-fold. As long as a molecular switch is successfully obtained, the secondary structure of the polypeptide can be destroyed or supported, thereby controlling the properties of the polypeptide.

Scientists at FMP's molecular switch embedded in polypeptides are in an extended form of the ground state, the so-called trans. This extension pattern keeps the two peptide chains separate from each other, preventing them from binding to form secondary structures. After irradiation with ultraviolet light at a wavelength of about 330 nanometers, the switch switches to cis, allowing hydrogen bonding between the two peptide chains. The polypeptide is then converted to the beta-type structure necessary for protein interaction and then binds to the specific position of the protein. The first author of the paper, Christie Hopman, explained that using this polypeptide model can control the corresponding natural protein interactions and then use light to control the corresponding signal chain.