Neuronal cells have different transporters, but how these transporters work is still a mystery. According to the report of the American Physicists Organization Network on April 24, American scientists have finally figured out the working mechanism of the transporter molecule recently, and the research was published in the journal Nature published on the 24th. Scientists say that the new research is expected to improve the treatment of mental illness and deepen the understanding of the principles of cocaine and other neuropharmaceuticals.

Transporters are molecular machines embedded in the membranes of neurons. Their role is to regulate signal transmission between nerve cells and recycle neurotransmitters. In the brain, neurons "talk" by releasing neurotransmitters to synapses (the junction of two neurons). In order to stop signal transmission, special transporters are needed to transport the neurotransmitters at the synapse back into the original cells. However, allowing neurotransmitters to accumulate at the synapse is of great benefit in the treatment of many diseases. Antidepressant drugs work by interfering with specific transport proteins to make neurotransmitters gather at synapses, as do stimulants such as cocaine and amphetamines.

In the latest experiment, a scientific research team led by Scott Blanchard, associate professor of physiology and biophysics at the Weill Cornell Medical College, used single-molecule fluorescence resonance energy transfer (smFRET) technology. A leucine transporter molecule (LeuT, which is very similar in structure and function to the mammalian neurotransmitter sodium transporter) was imaged to monitor changes in the composition and kinetics of LeuT and to explain the molecular activity within LeuT . They attached fluorescent dyes to the moving parts of the protein. When the distance between the dyes changed, the fluorescent dyes released different amounts of light. In the whole process, the movement of the transporter and the change of the distance between the fluorophores with time are directly imaged, thus giving a quantitative insight into the dynamics of the transport mechanism for the first time.

New experiments have shown that alanine attached to LeuT increases the rate at which the transporter changes between two forms: one form is facing outward, as if the transporter is ready to accept the matrix from outside the cell (closed inward). Another form is facing inward, as if the transporter releases the substance it contains towards the cell (opening inward). In addition, sodium is necessary for alanine to enhance this kinetic mechanism.

However, when there is only sodium ion and no alanine, the conversion rate between the on and off states of the transporter will decrease. The antidepressant clomipramine blocks this effect of alanine and restricts the transporter to its inwardly closed state to inhibit the transport process. Ariel Weinstein, director of the Computational Biomedical Research Institute at Weill Cornell Medical College, said that only by understanding this dynamics can we truly understand the working principle of drug molecules.

Weinstein said that because the transport proteins of bacteria and mammals are almost the same, the results of this study are likely to be applicable to transport proteins in mammals, including human nerve cells.

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