Inhibitor: Difference between revisions

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Latest revision as of 12:52, 18 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[edit]

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

Reversible Inhibitors[edit]

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[edit]

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

Competitive Inhibitors[edit]

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[edit]

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[edit]

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[edit]

References[edit]

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