Date published: 2026-5-5

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CD10 Inhibitors

CD10 inhibitors belong to a class of organic compounds that have demonstrated a remarkable ability to modulate the activity of the CD10 enzyme. CD10, also known as neprilysin or neutral endopeptidase, is a membrane-bound metallopeptidase primarily found on the surface of various cell types, including endothelial cells, immune cells, and neurons. This enzyme plays a crucial role in the degradation and regulation of numerous bioactive peptides, including hormones, neuropeptides, and cytokines. CD10 inhibitors are characterized by their specific binding interactions with the active site of the CD10 enzyme, thereby inhibiting its enzymatic activity. This class of compounds has garnered significant interest due to its implications in various physiological and pathological processes. Structurally, CD10 inhibitors often feature diverse chemical moieties, including heterocyclic rings, aromatic systems, and peptide-like fragments. These compounds typically possess functional groups that facilitate interactions with the active site residues of CD10. The binding of CD10 inhibitors to the enzyme's catalytic site results in a decrease in its enzymatic activity, which in turn leads to altered levels of various peptides involved in cellular signaling and regulation. The elucidation of the molecular interactions between CD10 inhibitors and the enzyme's active site has provided valuable insights into the development of compounds with enhanced affinity and specificity. The intricate interplay between the chemical structure of CD10 inhibitors and the enzyme's conformation guides the rational design of novel compounds with improved pharmacokinetic properties. The exploration of CD10 inhibitors continues to shed light on the broader roles of the CD10 enzyme in cellular homeostasis and disease processes. Ongoing research efforts aim to uncover the full scope of these inhibitors' effects on peptide regulation and their impact on various physiological functions.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Thiorphan (DL)

76721-89-6sc-201287
sc-201287A
5 mg
25 mg
$158.00
$413.00
5
(1)

Thiorphan (DL) acts as a potent inhibitor of CD10, engaging in specific interactions that disrupt peptide hydrolysis. Its unique structure facilitates selective binding to the enzyme's active site, effectively altering substrate affinity and enzymatic turnover. The compound's kinetic behavior reveals a nuanced modulation of proteolytic pathways, influencing the overall dynamics of peptide degradation. Additionally, Thiorphan's capacity to affect enzyme stability can lead to profound shifts in cellular regulatory networks.

Phosphoramidon

119942-99-3sc-201283
sc-201283A
5 mg
25 mg
$199.00
$632.00
8
(1)

Phosphoramidon serves as a selective inhibitor of CD10, characterized by its ability to form stable complexes with the enzyme. This interaction hinders the enzyme's catalytic activity, leading to altered kinetics in peptide metabolism. Its unique binding affinity allows for a distinct modulation of substrate interactions, impacting the overall proteolytic landscape. Furthermore, Phosphoramidon's influence on enzyme conformation can significantly affect downstream signaling pathways, highlighting its role in cellular regulation.

Racecadotril

81110-73-8sc-205831
sc-205831A
100 mg
500 mg
$54.00
$154.00
(1)

Racecadotril acts as a selective modulator of CD10, exhibiting unique interactions that alter enzyme dynamics. Its structure facilitates specific binding to the active site, resulting in a conformational shift that impacts substrate affinity. This modulation affects the enzyme's hydrolytic activity, leading to distinctive changes in peptide turnover rates. Additionally, Racecadotril's influence on enzyme stability can create a ripple effect in proteolytic processes, underscoring its role in biochemical pathways.

D-Phenylalanine

673-06-3sc-257292
sc-257292A
sc-257292B
sc-257292C
5 g
25 g
100 g
250 g
$24.00
$80.00
$156.00
$250.00
(0)

D-Phenylalanine serves as a selective inhibitor of CD10, engaging in unique molecular interactions that influence enzyme kinetics. Its structural conformation allows for precise binding to the enzyme's active site, inducing a notable alteration in catalytic efficiency. This interaction can modulate the enzyme's substrate specificity and turnover, thereby affecting the overall proteolytic landscape. The compound's stability and conformational flexibility further enhance its role in regulating enzymatic pathways.

Candoxatril

123122-55-4sc-504600
10 mg
$13500.00
(0)

Candoxatril is a CD10 inhibitor that was initially investigated for its potential in heart failure and hypertension. However, its development was discontinued due to limited efficacy.