Inhibitor: Difference between revisions

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Revision as of 15:00, 17 March 2025

Inhibitor is a substance that slows down or prevents a particular chemical reaction or other process, or that reduces the activity of a particular reactant, catalyst, or enzyme. It can refer to a substance that binds to an enzyme and decreases its activity. In the field of medicine and pharmacology, inhibitors are often used to treat various diseases and conditions.

Types of Inhibitors

There are several types of inhibitors, including reversible inhibitors, irreversible inhibitors, competitive inhibitors, and non-competitive inhibitors.

Reversible Inhibitors

Reversible inhibitors bind to enzymes with non-covalent interactions such as hydrogen bonds, hydrophobic interactions, and ionic bonds. These types of bonds are not permanent and can be reversed.

Irreversible Inhibitors

Irreversible inhibitors bind with the enzymes in a covalent bond and inactivate the enzyme permanently.

Competitive Inhibitors

Competitive inhibitors are inhibitors which form the shape of the substrate that is enzyme-specific. The enzymes are then occupied by the inhibitors and prevent the binding of the actual substrate.

Non-competitive Inhibitors

Non-competitive inhibitors bind to the enzyme at a different place other than the active site. In this type of inhibition, the structure of the enzyme is changed and it can no longer bind to the substrate.

Medical Uses

Inhibitors are used in medicine to treat a variety of conditions. For example, protease inhibitors are used to treat viral infections such as HIV and Hepatitis C. Angiotensin II receptor antagonists, which are a type of inhibitor, are used to lower blood pressure.

See Also

References

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