Date published: 2025-10-25

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Zfp871 Inhibitors

Zfp871 inhibitors represent a specialized class of molecules designed to modulate the activity of the zinc finger protein 871 (Zfp871), a transcription factor known for its role in regulating gene expression through its DNA-binding domains. Zinc finger proteins are a large family of proteins that use zinc ions to stabilize their structural domains and interact with nucleic acids. Zfp871, like other members of this family, contains multiple zinc finger motifs, which enable it to recognize specific DNA sequences and modulate the transcriptional activity of target genes. By inhibiting Zfp871, these molecules interfere with the protein's ability to bind to DNA and regulate gene expression, thereby altering the transcriptional profile of various cellular pathways. This can have far-reaching effects on biological systems, particularly in processes governed by gene regulation networks such as cell differentiation, proliferation, and apoptosis.

The development of Zfp871 inhibitors involves understanding the molecular architecture of the zinc finger motifs and their interaction with nucleic acids. This often requires detailed structural studies using techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy to elucidate the binding sites and conformational changes associated with inhibitor binding. Additionally, the selectivity of these inhibitors is crucial, as zinc finger proteins share common structural elements, making it essential to design inhibitors that specifically target Zfp871 without affecting other zinc finger proteins. Molecular docking and computational chemistry methods are frequently employed to refine the interactions between inhibitors and Zfp871, ensuring precise and effective inhibition. Research into this class of inhibitors thus focuses heavily on the structural biology, biochemistry, and molecular dynamics of Zfp871, as well as the broader implications of modulating zinc finger protein-mediated gene regulation.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Disulfiram

97-77-8sc-205654
sc-205654A
50 g
100 g
$52.00
$87.00
7
(1)

Disulfiram inhibits the activity of metalloenzymes by chelating metal ions, leading to inhibition of zinc finger protein 871, which relies on zinc for its structural integrity and function.

Clioquinol

130-26-7sc-201066
sc-201066A
1 g
5 g
$44.00
$113.00
2
(1)

Clioquinol chelates zinc, therefore inhibiting zinc finger protein 871 by removing the essential zinc ions necessary for its structural configuration and DNA-binding activity.

Zinc

7440-66-6sc-213177
100 g
$47.00
(0)

Pyrithione Zinc chelates zinc ions, which could inhibit the DNA-binding activity of zinc finger protein 871 by disrupting its zinc finger domain necessary for its function.

TPEN

16858-02-9sc-200131
100 mg
$127.00
10
(3)

TPEN is a high-affinity zinc chelator that can sequester zinc ions, leading to the functional inhibition of zinc finger protein 871 by depriving it of its zinc cofactor.

Phytic acid solution

83-86-3sc-205806
sc-205806A
100 ml
500 ml
$148.00
$505.00
(0)

Phytic acid binds to and sequesters metal ions including zinc, which can inhibit zinc finger protein 871 by disrupting the metal ion homeostasis it requires for function.

Dithizone

60-10-6sc-206031A
sc-206031
10 g
50 g
$90.00
$332.00
2
(0)

Dithizone is a chelating agent for heavy metal ions including zinc, which can inhibit zinc finger protein 871 by removing zinc ions critical for its structural and functional integrity.

L-Mimosine

500-44-7sc-201536A
sc-201536B
sc-201536
sc-201536C
25 mg
100 mg
500 mg
1 g
$35.00
$86.00
$216.00
$427.00
8
(2)

Mimosine chelates metal ions, and its chelation of zinc can result in the inhibition of zinc finger protein 871 by disrupting the zinc-dependent domains essential for its activity.

1,10-Phenanthroline

66-71-7sc-255888
sc-255888A
2.5 g
5 g
$23.00
$31.00
(0)

1,10-Phenanthroline is a metal ion chelator that can inhibit zinc finger protein 871 by binding to zinc ions, which are necessary for the protein's structure and function.