Steroids include steroid hormones such as cortisol, estrogen, and testosterone. In fact, all steroid hormones are made from chemical changes in the basic structure of cholesterol. At about making a molecule of molecular conversion easier, scientists call it synthetic.
Hypercholesterolemia means that the levels of cholesterol in the blood is too high.
Cholesterol can be made synthetically. Cholesterol synthetic currently implemented in widescreen technology (billboards) as an alternative to the LCD.
High levels of cholesterol in the body to trigger the emergence of a variety of diseases. Healthy eating is a key factor for mengghindari this. However, not all cholesterol is bad for the body. Only the category of LDL cholesterol are bad while the type of cholesterol [HDL] cholesterol is the bad cholesterol that can dissolve in the body. Normal cholesterol is 160-200 mg. High cholesterol levels can be lowered by simvastatin.
Inhibiting Cholesterol Forming Enzyme Performance
The researchers have determined the structure and mechanism of action of an enzyme that plays an important role in the initial formation of cholesterol and bacterial virulence factors staph. Staph bacteria are a group of bacteria that colonize that resemble a sprig of grapes.
Chemists from the University of Illinois and collaborators from Taiwan studied a type of enzyme found in humans, plants, fungi, parasites, and many types of bacteria that initiate the formation of one molecule triterpena-the oldest and most abundant chemical on earth. Triterpena a precursor to the formation of steroids such as cholesterol.
"These enzymes are important drug targets," said Professor Eric Oldfield, a professor of chemistry at the University of Illinois. "Inhibiting the activity of this enzyme can lead us to the discovery of cholesterol-lowering drugs, antibiotics that can treat bacterial infections, and drugs that can attack the parasites that cause tropical diseases such as Chagas plague - a plague that causes sudden death in Latin America."
For this experiment, the research team took samples corresponding enzyme, dehydrosqualene synthase (CrtM) from the bacterium Staphylococcus aureus. Staph bacteria is a common type of bacteria that can cause infections, which are notoriously difficult to eradicate. The mechanism of infection caused by these bacteria is the formation of the so-called golden sheath staphyloxanthin that protects the bacteria from the human immune system. CrtM staphyloxanthin catalyzes the initial reaction formation, by inhibiting the action of enzymes that will make the bacteria does not have a protective sheath and ultimately became vulnerable to attack by white blood cells as antibodies our bodies.
Researchers previously have known CrtM shape and final products are formed, but they do not know how these enzymes work. By understanding the mechanism of action of this enzyme will allow researchers to design better inhibitors, and can even customize it to another target.
The team managed to crystallize the enzyme to be analyzed. Then they studied the structure of the enzyme complex by X-ray crystallography using synchrotron located at the Advanced Photon Source at Argonne National Laboratory. They found that the two-stage reaction CrtM show, releasing two diphosphate groups from the substrate. Substrate changed between two active side of the enzyme as the reaction proceeds. The most effective inhibitors that can bind strongly to both the active site of the enzyme to inhibit the action of enzymes as a whole.
"Human beings have developed ways to cope with diseases like this, but never had a clear structural basis," said Professor Oldfield, who is also a professor of biophysics at the same institution. "But now that we can see how the protein works, we have been in a much better position to design molecules that can fight bacterial infections and parasitic outbreaks more effectively, and also has the potential to lower cholesterol."
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