DIDS
DIDS (4,4'-Diisothiocyanatostilbene-2,2'-disulfonic acid) is a chemical compound used as an inhibitor in the field of biochemistry. It is often used to inhibit anion exchange proteins, including Band 3 and chloride channels.
Structure and Properties[edit | edit source]
DIDS is a disulfonic acid derivative of stilbene. It is a yellow solid that is soluble in water. The compound has a molecular weight of 466.42 g/mol and a melting point of 300 °C.
Uses[edit | edit source]
In biochemistry, DIDS is used as an inhibitor of anion exchange proteins. It is known to inhibit Band 3, a protein that mediates the exchange of chloride and bicarbonate across the plasma membrane of cells. DIDS is also used to inhibit chloride channels, which are integral membrane proteins that allow chloride ions to pass along their electrochemical gradient.
Mechanism of Action[edit | edit source]
DIDS inhibits anion exchange proteins by binding to their extracellular domain. This binding prevents the proteins from undergoing the conformational changes necessary for ion transport. The inhibition of chloride channels by DIDS is thought to occur through a similar mechanism.
Side Effects and Risks[edit | edit source]
While DIDS is a useful tool in biochemical research, it is not without risks. The compound is known to be toxic if ingested or inhaled, and it can cause skin and eye irritation. Therefore, it should be handled with care in the laboratory.
See Also[edit | edit source]
DIDS Resources | |
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