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Scientists from the University of the Northwest, in the united States, have discovered a new weak point in the famous protein S or protein of the espícula , the major molecule by which the SARS-CoV-2 recognizes human cells and enters them. The finding opens a new possible way of treatment and has been recently published in the journal “ACS Nano”.

through simulations that reproduced the protein at a scale of nanometers (a nanometer is one-millionth of a millimeter), the researchers analysed a region with positive charge, known as cleavage site polybasic . This area is located at a distance of 10 nanometers from the recognition site of the S protein, the exact point in which the molecule binds to the human proteins. Such as have been found, this cleavage allows the binding between the protein of the espícula and recipients of human cells, with a negative charge, to be strong.

For that, they have designed a molecule which is negative with ability to bind to the cleavage, thus blocking the ability of SARS-CoV-2 to bind to human cells .

A possible treatment

“Our work indicates that block this cleavage site can be a prophylactic treatment feasible to decrease the ability of the virus to infect humans,” he said in a press release Monica Olvera de la Cruz , director of research. “In addition, our results explain experimental studies showing that mutations of the protein of the espícula affecting the transmissibility of the virus”.

This cleavage site had been elusive up to now and according to the researchers has been a big surprise to find out its location and its ability to interact on the site of union, by which the protein of the virus binds the human receptor.

did Not expect to find electrostatic interactions to a distance of 10 nanometers,” said Baofu Qiao, first author of the study. “Under physiological conditions, this type of interaction does not often occur more of a nanometer”.

In this case it seems to be not so. As explained Olvera Cruz, everything indicates that this region attaches to an enzyme named furin, very abundant in the lungs , “suggesting that the cleavage site is crucial for the virus entry in human cells.”

With this information in hand, Olvera de la Cruz and Qiao plan to work with chemists and pharmacologists to develop a new treatment to this region of the protein of the espícula.

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