Date published: 2025-10-31

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uPA Inhibitors

Urokinase-type plasminogen activator (uPA) inhibitors represent a class of chemical compounds that function by selectively inhibiting the enzymatic activity of uPA, a serine protease. uPA plays a pivotal role in the conversion of plasminogen to plasmin, a key enzyme in the fibrinolytic system responsible for the degradation of fibrin and other extracellular matrix components. The inhibition of uPA disrupts this conversion process, thereby influencing various biological processes that rely on proteolytic cascades. The chemical structures of uPA inhibitors are diverse, ranging from small molecules to peptides, each designed to target the active site or the zymogen activation pathway of uPA. These inhibitors often exhibit a high degree of specificity and affinity for uPA due to the precise molecular interactions within the protease's active site, including hydrogen bonding, hydrophobic interactions, and sometimes covalent binding. Chemically, uPA inhibitors can be classified into several subclasses based on their mode of interaction with the enzyme. Some inhibitors act as competitive inhibitors by mimicking the natural substrate of uPA and binding to its active site, thus blocking substrate access. Others may function as allosteric inhibitors, binding to a different site on the enzyme and inducing conformational changes that reduce enzymatic activity. Additionally, there are irreversible inhibitors that form a covalent bond with the enzyme, leading to permanent inactivation. The design and synthesis of uPA inhibitors involve complex chemical strategies, often incorporating structure-activity relationship (SAR) studies to optimize the inhibitory potency and selectivity. The physicochemical properties of these inhibitors, such as solubility, stability, and permeability, are also critical factors in their effectiveness as enzyme inhibitors. These compounds provide valuable tools for studying the mechanistic roles of uPA in various biological processes, offering insights into the regulation of proteolytic systems and the intricate balance of extracellular matrix remodeling.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Amiloride hydrochloride dihydrate

17440-83-4sc-364401
250 mg
$77.00
1
(0)

Inhibits uPA by directly interacting with its active site, leading to reduced proteolytic activity involved in tissue remodeling and invasion.

uPA Inhibitor II, UK122

1186653-73-5sc-356185
5 mg
$360.00
5
(2)

uPA Inhibitor II, UK122, is a selective inhibitor that interacts with the urokinase-type plasminogen activator (uPA) through specific binding to its active site. This compound exhibits unique conformational flexibility, allowing it to stabilize the enzyme in an inactive state. Its distinct molecular interactions, including hydrogen bonding and hydrophobic contacts, can significantly alter the kinetics of plasminogen activation, influencing proteolytic pathways and cellular signaling mechanisms.

Amiloride • HCl

2016-88-8sc-3578
sc-3578A
25 mg
100 mg
$22.00
$56.00
6
(2)

Amiloride • HCl acts as a potent uPA inhibitor by engaging in specific interactions with the enzyme's active site, effectively modulating its activity. The compound's unique structural features facilitate strong electrostatic interactions and hydrophobic stacking, which can lead to altered reaction kinetics. This modulation impacts the dynamics of proteolytic cascades, influencing various cellular processes and signaling pathways through its selective binding affinity.

Amiloride

2609-46-3sc-337527
1 g
$290.00
7
(1)

Amiloride exhibits unique characteristics as a uPA inhibitor, primarily through its ability to form stable complexes with the enzyme. Its distinct molecular architecture allows for precise alignment within the active site, enhancing binding affinity. The compound's hydrophilic regions promote solvation effects, while its aromatic moieties contribute to π-π interactions, influencing the overall stability of the enzyme-substrate complex. This interplay alters the kinetics of proteolytic activity, impacting downstream signaling mechanisms.

1,5-Dansyl-Glu-Gly-Arg Chloromethyl Ketone, Dihydrochloride

sc-220558
5 mg
$462.00
(0)

1,5-Dansyl-Glu-Gly-Arg Chloromethyl Ketone, Dihydrochloride acts as a uPA inhibitor by engaging in specific interactions with the enzyme's active site. Its unique structure facilitates the formation of covalent bonds, leading to irreversible inhibition. The presence of dansyl groups enhances fluorescence properties, allowing for real-time monitoring of enzyme activity. Additionally, the compound's hydrophobic regions contribute to its membrane permeability, influencing cellular uptake and localization.

N-alpha-Benzoyl-L-argininamide hydrochloride

4299-03-0sc-301278
sc-301278A
5 g
25 g
$93.00
$270.00
(0)

N-alpha-Benzoyl-L-argininamide hydrochloride functions as a uPA inhibitor through its ability to form stable complexes with the enzyme, disrupting its catalytic activity. The benzoyl moiety enhances hydrophobic interactions, promoting binding affinity. Its amide linkage contributes to conformational rigidity, influencing the kinetics of enzyme-substrate interactions. Furthermore, the compound's solubility characteristics facilitate its diffusion across biological membranes, impacting its distribution within cellular environments.

GGACK

65113-67-9sc-201314
sc-201314A
sc-201314B
5 mg
25 mg
100 mg
$315.00
$1375.00
$5000.00
(1)

GGACK acts as a uPA inhibitor by engaging in specific non-covalent interactions with the enzyme's active site, effectively hindering its proteolytic function. The unique structural features of GGACK allow for enhanced electrostatic interactions, which stabilize the enzyme-inhibitor complex. Additionally, its distinct steric properties influence the conformational dynamics of uPA, altering the reaction kinetics and potentially modulating downstream signaling pathways. The compound's solubility profile also plays a crucial role in its bioavailability and interaction with cellular components.

uPA Inhibitor Inhibitor

149732-36-5sc-356184
5 mg
$311.00
1
(0)

uPA Inhibitor functions by selectively binding to the active site of uPA, disrupting its enzymatic activity through precise molecular interactions. Its unique conformation promotes strong hydrogen bonding and hydrophobic contacts, which stabilize the inhibitor-enzyme complex. This binding alters the enzyme's structural dynamics, affecting its catalytic efficiency and influencing the kinetics of substrate turnover. Furthermore, the inhibitor's physicochemical properties enhance its affinity for uPA, impacting its overall efficacy in modulating proteolytic processes.

BC 11 hydrobromide

443776-49-6sc-362712
sc-362712A
10 mg
50 mg
$306.00
$1224.00
(0)

Specifically inhibits uPA activity, thereby impacting processes like cell migration and invasion associated with uPA.

4-Chlorophenylguanidine hydrochloride

14279-91-5sc-203474
100 mg
$250.00
(0)

4-Chlorophenylguanidine hydrochloride exhibits a distinctive mechanism of action as a uPA inhibitor by engaging in specific electrostatic interactions with the enzyme's active site. Its unique molecular structure facilitates the formation of a stable complex, effectively hindering substrate access. The compound's hydrophilic and lipophilic balance influences its solubility and distribution, while its kinetic profile reveals a competitive inhibition pattern, altering the enzyme's activity and impacting proteolytic pathways.