Date published: 2026-5-8

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sPLA2 Inhibitors

Chemical inhibitors of sPLA2 offer a variety of mechanisms by which they impede the protein's function. Indoxam operates by directly binding to the active site of sPLA2, effectively preventing the enzyme from interacting with phospholipid substrates it typically hydrolyzes. Similarly, Varespladib acts as a competitive inhibitor, engaging with the catalytic site to block substrate access, while LY315920 selectively binds to the same site, ensuring that the enzyme's activity is inhibited. Darapladib takes a comparable approach, attaching to sPLA2 and thus inhibiting the crucial enzymatic activity responsible for releasing arachidonic acid, which is a precursor for pro-inflammatory eicosanoids. The inhibition strategy continues with Anthera (A-001), which targets sPLA2 directly to prevent its function in the inflammatory response, by halting the release of arachidonic acid from phospholipids. Methyl arachidonyl fluorophosphonate covalently modifies the active site of sPLA2, leading to irreversible inhibition and impeding the inflammatory cascade. Arachidonyl trifluoromethyl ketone and Bromoenol lactone both function by preventing the release of fatty acids and lysophospholipids, with the former being a selective inhibitor and the latter binding irreversibly to the enzyme. Rosmanol interacts with sPLA2 to inhibit its activity, consequently reducing the production of inflammatory mediators from the arachidonic acid pathway. Manoalide also forms a covalent bond with sPLA2, ensuring that the enzyme's role in the liberation of arachidonic acid is blocked. Efipladib, in a similar vein, occupies the active site of sPLA2, selectively inhibiting its function in mediating inflammation. Lastly, Propantheline indirectly inhibits sPLA2 by reducing intracellular calcium levels through the blockade of muscarinic receptors, calcium being a necessary factor for sPLA2 activation and consequent inflammatory responses.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

LY315920

172732-68-2sc-364528
sc-364528A
5 mg
10 mg
$315.00
$490.00
(1)

LY315920 acts as a selective sPLA2 inhibitor, engaging with the enzyme through specific hydrophobic and electrostatic interactions that stabilize its binding. This compound alters the hydrolysis of phospholipids, impacting lipid metabolism and inflammatory pathways. Its unique kinetic properties reveal a non-competitive inhibition mechanism, leading to a distinct modulation of arachidonic acid release. The compound's structural characteristics promote unique conformational dynamics within the enzyme, influencing its overall activity.

Oleyloxyethyl Phosphorylcholine

96720-06-8sc-200711
sc-200711A
10 mg
50 mg
$80.00
$283.00
6
(0)

Oleyloxyethyl Phosphorylcholine exhibits a distinctive role as a sPLA2 modulator, characterized by its ability to form strong hydrogen bonds and hydrophobic interactions with the enzyme's active site. This compound influences the enzymatic hydrolysis of phospholipids, thereby affecting membrane integrity and signaling pathways. Its reaction kinetics suggest a unique allosteric modulation, altering substrate affinity and enzymatic turnover rates, which can lead to significant changes in lipid-derived signaling molecules.

7,7-Dimethyleicosadienoic Acid (DEDA)

89560-01-0sc-200707
sc-200707A
10 mg
50 mg
$99.00
$364.00
(0)

7,7-Dimethyleicosadienoic Acid (DEDA) acts as a potent sPLA2 modulator, showcasing unique interactions with the enzyme's catalytic site. Its structural features facilitate specific van der Waals forces and electrostatic interactions, enhancing substrate binding efficiency. DEDA's influence on lipid metabolism is evident through its ability to alter reaction kinetics, promoting distinct pathways in phospholipid turnover and impacting downstream signaling cascades. This compound's behavior underscores its role in lipid dynamics and cellular responses.

Luffariellolide

111149-87-2sc-202212
1 mg
$263.00
(1)

Luffariellolide exhibits remarkable specificity as an sPLA2 inhibitor, engaging in unique hydrogen bonding and hydrophobic interactions with the enzyme's active site. Its structural conformation allows for selective modulation of phospholipid hydrolysis, influencing the kinetics of substrate turnover. This compound also alters membrane fluidity, which can affect enzyme accessibility and activity, thereby shaping lipid signaling pathways and cellular membrane dynamics in a distinctive manner.

Thioetheramide PC

116457-99-9sc-202840
sc-202840A
5 mg
25 mg
$64.00
$321.00
(0)

Thioetheramide PC acts as a potent sPLA2 modulator, characterized by its ability to form stable complexes with the enzyme through unique electrostatic interactions. Its distinct molecular architecture facilitates selective binding, influencing the catalytic efficiency and substrate affinity. Additionally, Thioetheramide PC can alter lipid bilayer properties, impacting membrane permeability and fluidity, which may lead to significant changes in cellular signaling and lipid metabolism pathways.

4-[(1-oxo-7-phenylheptyl)amino]-(4R)-octanoic acid

1101136-50-8sc-223602
sc-223602A
1 mg
5 mg
$39.00
$231.00
(0)

4-[(1-oxo-7-phenylheptyl)amino]-(4R)-octanoic acid exhibits unique interactions with sPLA2, enhancing its enzymatic activity through specific hydrophobic and hydrogen bonding interactions. This compound's structural features allow it to modulate the enzyme's conformation, potentially affecting substrate access and turnover rates. Furthermore, it influences lipid dynamics within membranes, which may alter the local microenvironment and impact downstream signaling cascades.