Protein research is one of the hottest
areas of medical research because protein-based drugs can be developed to treat
diabetes, cancer and other diseases.
Although proteins have great potential,
their incredibly complex chemical structures pose enormous challenges for
scientists. As a result, researchers have been looking for a tool to modify
them more precisely, thereby reducing the side effects of the drug.
Recently, researchers have developed a new
protein modification method that can reduce the side effects of drugs and can
be the key to promoting the development of protein drugs. Their research has
been published in Nature Communications.
Protein structure is like an intricate yarn
ball
Researchers call this method "His-tag
acetylation." In addition, it can add toxic molecules to proteins that
attack diseased cells in the body of cancer without attacking healthy cells.
“Protein is like a ball of yarn. When they
are opened, a long chain of amino acids will appear. This new modification
allows us to precisely target these intricate structures. In short, it will
help the drug production, and we can make changes more confidently so that we
can reduce side effects in the future," the author said.
Modified proteins must be pinpointed
His-tag acylation accurately targets these
complex yarn-like protein structures, which also makes it possible to produce
drugs with novel properties.
For example, researchers can now attach
fluorescent molecules to proteins, allowing microscopy to track the path of
proteins through cells. Since the primary function of these proteins is to
transport anticancer molecules around the diseased cells, it is important to
follow their path carefully throughout the body.
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