Date published: 2026-5-30

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Metallothionein 1G Inhibitors

Chemical inhibitors of Metallothionein 1G can exert their inhibitory effects through direct interaction with the protein's metal-binding sites. Cadmium chloride, for example, binds to Metallothionein 1G, sequestering the protein and inhibiting its ability to bind essential metals, crucial for its detoxification and metal buffering roles. Similarly, Mercury(II) chloride targets the sulfhydryl groups of Metallothionein 1G, inhibiting its metal-binding capacity, which disrupts its function in cellular metal ion regulation. Silver nitrate reacts with the thiol groups within Metallothionein 1G, leading to the inactivation of its zinc and copper ion regulation ability. Lead(II) acetate and Bismuth(III) nitrate also bind to the thiol groups of Metallothionein 1G, inhibiting its normal function and disrupting metal homeostasis within the cell.

Other metal ions, such as those from Copper(II) sulfate and Zinc chloride, can saturate Metallothionein 1G's metal-binding sites, inhibiting its regulatory function in zinc homeostasis and attenuating its protective role in metal detoxification. Nickel(II) sulfate and Cobalt(II) chloride both compete with physiological metal ions for binding to Metallothionein 1G, disrupting its homeostatic function and its role in metal toxicity protection. Cisplatin, a well-known platinum compound, forms adducts with the thiol groups of Metallothionein 1G, blocking the essential metal ion binding sites, impairing the protein's detoxification capacity. Finally, Gold(III) chloride forms stable complexes with the sulfur atoms in Metallothionein 1G, inhibiting its metal ion binding and storage functions, which interferes with its cellular defense against metal toxicity.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Cadmium chloride, anhydrous

10108-64-2sc-252533
sc-252533A
sc-252533B
10 g
50 g
500 g
$56.00
$183.00
$352.00
1
(1)

Cadmium chloride directly binds to Metallothionein 1G, resulting in the sequestration of the protein and inhibiting its ability to bind essential metals, thereby inhibiting its metal buffering and detoxification functions.

Silver nitrate

7761-88-8sc-203378
sc-203378A
sc-203378B
25 g
100 g
500 g
$114.00
$378.00
$1081.00
1
(1)

Silver nitrate reacts with the thiol groups in Metallothionein 1G, inactivating its capacity to bind and regulate zinc and copper ions within the cell.

Lead(II) Acetate

301-04-2sc-507473
5 g
$85.00
(0)

Lead(II) acetate interacts with Metallothionein 1G by binding to its thiol groups, which inhibits the protein's normal metal-binding function and disrupts metal homeostasis.

Copper(II) sulfate

7758-98-7sc-211133
sc-211133A
sc-211133B
100 g
500 g
1 kg
$46.00
$122.00
$189.00
3
(1)

Copper(II) sulfate can bind preferentially to Metallothionein 1G, which can inhibit the protein's regulatory role in zinc metabolism and its protective effects against copper toxicity.

Zinc

7440-66-6sc-213177
100 g
$48.00
(0)

Zinc chloride can saturate the metal-binding sites of Metallothionein 1G, inhibiting its regulatory function in zinc homeostasis and attenuating its protective role in metal detoxification.

Nickel Sulfate

7786-81-4sc-507407
5 g
$63.00
(0)

Nickel(II) sulfate can bind to Metallothionein 1G, leading to an inhibition of its metal-binding sites, which disrupts its function in metal ion homeostasis and protection against metal toxicity.

Cobalt(II) chloride

7646-79-9sc-252623
sc-252623A
5 g
100 g
$64.00
$176.00
7
(1)

Cobalt(II) chloride competes with physiological metal ions for binding to Metallothionein 1G, inhibiting the protein's metal-binding capacity and its role in the maintenance of metal ion equilibrium.

Cisplatin

15663-27-1sc-200896
sc-200896A
100 mg
500 mg
$138.00
$380.00
101
(4)

Cisplatin forms adducts with the thiol groups of Metallothionein 1G, which inhibits its function by blocking the binding sites for essential metal ions, thereby impairing its detoxification capacity.

Gold(III) chloride

13453-07-1sc-250066
250 mg
$56.00
(0)

Gold(III) chloride can form stable complexes with the sulfur atoms in Metallothionein 1G, inhibiting its metal ion binding and storage functions and interfering with its role in cellular defense against metal toxicity.