Date published: 2025-10-15

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MAO-B Inhibitors

Monoamine oxidase B (MAO-B) is an enzyme predominantly located in the outer mitochondrial membrane of glial cells in the central nervous system, as well as in peripheral tissues. It plays a crucial role in the catabolism of monoamine neurotransmitters such as dopamine, phenylethylamine, and benzylamine, thereby regulating their levels within the synaptic cleft and influencing neural activity and neuromodulation. The function of MAO-B extends beyond the mere breakdown of monoamines; it is also involved in the generation of reactive oxygen species as by-products of the deamination process, which has implications for oxidative stress and neuronal aging. The regulation of MAO-B activity is, therefore, of significant interest in the context of neurological function and dysfunction, with its activity finely balanced to ensure optimal levels of monoamine neurotransmitters are maintained for proper neuronal communication and plasticity. Dysregulation of MAO-B activity can lead to altered monoaminergic signaling, implicated in various neuropsychiatric and neurodegenerative disorders, underscoring the enzyme's critical role in brain health. The inhibition of MAO-B is a process that directly impacts the enzyme's ability to catalyze the oxidative deamination of monoamine neurotransmitters, leading to increased availability of these neurochemicals in the synaptic cleft. Inhibition can occur through different mechanisms, including competitive, non-competitive, and irreversible binding to the enzyme's active site. These interactions block MAO-B from accessing its substrates, effectively reducing the rate of monoamine catabolism and the associated production of hydrogen peroxide, a by-product of the deamination reaction. This decrease in monoamine breakdown and reactive oxygen species generation can have significant implications for neuronal signaling and oxidative stress. The specific inhibition of MAO-B, as opposed to MAO-A, offers a targeted approach to modulate the monoaminergic system, particularly dopaminergic signaling, without substantially affecting the metabolism of other neurotransmitters like serotonin. Understanding the molecular basis of MAO-B inhibition allows for the exploration of regulatory mechanisms that could influence neurophysiological processes and neuroprotection, highlighting the enzyme's importance in neural health and the consequences of its altered activity.

Items 1 to 10 of 25 total

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Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Quinacrine, Dihydrochloride

69-05-6sc-204222
sc-204222B
sc-204222A
sc-204222C
sc-204222D
100 mg
1 g
5 g
200 g
300 g
$45.00
$56.00
$85.00
$3193.00
$4726.00
4
(2)

Quinacrine, Dihydrochloride exhibits intriguing characteristics as a selective inhibitor of monoamine oxidase B (MAO-B). Its unique structural features enable it to engage in specific hydrogen bonding and hydrophobic interactions with the enzyme, influencing its catalytic efficiency. The compound's amphiphilic nature enhances its ability to traverse lipid membranes, potentially affecting the localization and activity of neurotransmitter substrates, thereby impacting their metabolic pathways.

Tranylcypromine

13492-01-8sc-200572
sc-200572A
1 g
5 g
$172.00
$587.00
5
(1)

Tranylcypromine functions as a selective inhibitor of monoamine oxidase B (MAO-B), showcasing distinctive molecular interactions that modulate enzyme activity. Its unique stereochemistry allows for effective binding to the active site, altering the enzyme's conformation and reaction kinetics. The compound's lipophilic characteristics facilitate its penetration into cellular environments, potentially influencing the dynamics of neurotransmitter degradation and the overall metabolic landscape within neuronal pathways.

cis-Resveratrol Solution (in Ethanol)

61434-67-1sc-205254
sc-205254A
5 mg
10 mg
$120.00
$228.00
2
(1)

Cis-Resveratrol Solution in ethanol exhibits intriguing interactions with monoamine oxidase B (MAO-B), characterized by its ability to stabilize enzyme conformations through specific hydrogen bonding and hydrophobic interactions. This compound's unique structural features enhance its affinity for the enzyme, leading to altered reaction kinetics. Additionally, its solubility in ethanol promotes efficient cellular uptake, potentially impacting metabolic processes and signaling pathways within the brain.

Rasagiline

136236-51-6sc-204875
sc-204875A
25 mg
100 mg
$101.00
$210.00
(1)

Rasagiline functions as an irreversible MAO-B inhibitor by forming a covalent bond with the enzyme. This covalent modification renders the enzyme inactive and unable to perform its role in the degradation of neurotransmitters.

Quinacrine Dihydrochloride Dihydrate

6151-30-0sc-391946B
sc-391946C
sc-391946
sc-391946A
1 g
5 g
10 g
25 g
$42.00
$84.00
$161.00
$338.00
1
(0)

Quinacrine Dihydrochloride Dihydrate demonstrates notable interactions with monoamine oxidase B (MAO-B) through its unique ability to form ionic bonds and engage in π-π stacking with aromatic residues. This compound's distinct electronic configuration facilitates rapid electron transfer, influencing the enzyme's catalytic efficiency. Its crystalline structure enhances stability, while the dihydrate form contributes to solubility, allowing for effective diffusion in biological systems.

trans 2-Phenylcyclopropylamine Hydrochloride

1986-47-6sc-208452
sc-208452A
250 mg
1 g
$56.00
$163.00
1
(0)

Trans 2-Phenylcyclopropylamine Hydrochloride exhibits intriguing interactions with monoamine oxidase B (MAO-B) by forming hydrogen bonds and engaging in hydrophobic interactions with the enzyme's active site. Its cyclopropyl moiety introduces strain, enhancing binding affinity and altering reaction kinetics. The compound's unique stereochemistry allows for selective inhibition, while its hydrochloride form improves solubility, promoting effective interaction dynamics within biochemical pathways.

R(−)-Deprenyl hydrochloride

14611-52-0sc-200742
sc-200742A
sc-200742B
100 mg
250 mg
1 g
$32.00
$77.00
$281.00
(1)

R(-)-Deprenyl hydrochloride acts as a selective inhibitor of monoamine oxidase B (MAO-B), showcasing unique binding characteristics due to its asymmetric structure. The compound's hydrophobic regions facilitate strong interactions with the enzyme, while its specific stereochemistry enhances its affinity for the active site. This selective inhibition alters the enzymatic reaction kinetics, allowing for a nuanced modulation of neurotransmitter metabolism, which can influence various biochemical processes.

cis-Resveratrol

61434-67-1sc-363863
sc-363863A
10 mg
100 mg
$340.00
$2400.00
2
(0)

Cis-Resveratrol exhibits intriguing interactions with monoamine oxidase B (MAO-B) through its polyphenolic structure, which allows for multiple hydrogen bonding and π-π stacking with the enzyme's active site. This compound's unique conformation promotes selective binding, influencing the enzyme's catalytic efficiency. Additionally, its antioxidant properties may modulate oxidative stress pathways, further impacting MAO-B activity and related metabolic processes.

Ro 16-6491

94319-79-6sc-200743
sc-200743A
200 mg
1 g
$57.00
$218.00
(0)

Ro 16-6491 demonstrates a distinctive affinity for monoamine oxidase B (MAO-B) through its unique structural features, which facilitate specific hydrophobic interactions and electrostatic complementarity with the enzyme's active site. This compound exhibits a notable ability to stabilize the enzyme-substrate complex, thereby altering reaction kinetics. Its conformational flexibility allows for dynamic adjustments during binding, potentially influencing the enzyme's overall activity and regulatory mechanisms.

Pargyline hydrochloride

306-07-0sc-215676
sc-215676A
500 mg
1 g
$39.00
$82.00
2
(1)

Pargyline hydrochloride exhibits a selective interaction with monoamine oxidase B (MAO-B), characterized by its ability to form stable hydrogen bonds and hydrophobic contacts within the enzyme's active site. This compound's unique steric configuration enhances its binding affinity, leading to a modulation of the enzyme's catalytic efficiency. Additionally, its electronic properties may influence the redox state of the enzyme, impacting the overall metabolic pathways associated with neurotransmitter degradation.