Date published: 2026-5-17

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CFTR Inhibitors

CFTR inhibitors belong to a specific chemical class of compounds meticulously designed to modulate the activity of the CFTR protein. CFTR, or cystic fibrosis transmembrane conductance regulator, is a chloride ion channel protein that is crucial for regulating ion transport across cell membranes, particularly in epithelial cells. These inhibitors are thoughtfully crafted molecules engineered to interact with the CFTR protein, influencing its normal function. Through these interactions, they might impact various cellular processes associated with ion transport, fluid balance, and cellular responses, without directly altering its ion-conducting domains or its involvement in ion channel activities. The design of CFTR inhibitors is grounded in a comprehensive understanding of the structural and functional attributes of the CFTR protein. Typically developed using advanced chemical synthesis methods and informed by insights from cell biology and ion channel physiology, these inhibitors are characterized by their ability to selectively bind to CFTR. This selectivity enables focused modulation of cellular pathways that rely on the activity of this specific protein. Unraveling the intricacies of ion transport, fluid homeostasis, and cellular interactions often employ CFTR inhibitors as valuable tools. The development and utilization of CFTR inhibitors contribute to advancing our knowledge of the complex interplay between cellular components and ion dynamics, offering insights into the fundamental molecular mechanisms that govern ion transport and contribute to cellular responses to changes in ion channel activities.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Glyburide (Glibenclamide)

10238-21-8sc-200982
sc-200982A
sc-200982D
sc-200982B
sc-200982C
1 g
5 g
25 g
100 g
500 g
$46.00
$61.00
$117.00
$173.00
$530.00
36
(1)

Glyburide, a sulfonylurea derivative, demonstrates intriguing interactions with the CFTR channel, particularly in modulating its conductance. Its specific binding affinity to the channel's nucleotide-binding domains can alter conformational states, influencing chloride ion flow. The compound's hydrophobic regions promote membrane integration, while its polar functionalities enhance solubility in biological systems. This duality allows for nuanced effects on cellular ion homeostasis and transport kinetics.

CFTR Inhibitor-172

307510-92-5sc-204680
sc-204680A
10 mg
50 mg
$168.00
$520.00
10
(1)

CFTR Inhibitor-172 is a selective compound that interacts with the CFTR protein, specifically targeting its regulatory domains. This inhibitor disrupts the channel's gating mechanisms, leading to altered ion transport dynamics. Its unique structure facilitates specific hydrogen bonding and hydrophobic interactions, which can stabilize certain conformations of the CFTR protein. The compound's kinetic profile suggests a rapid onset of action, influencing chloride ion permeability and cellular ion balance.

Ivacaftor

873054-44-5sc-364679
5 mg
$259.00
(1)

Ivacaftor is a CFTR potentiator that enhances chloride channel activity by binding to the CFTR protein and improving its function at the cell surface.

PPQ-102

931706-15-9sc-364673
10 mg
$298.00
1
(1)

PPQ-102 is a potent modulator of the CFTR protein, exhibiting unique binding characteristics that enhance its interaction with the channel's nucleotide-binding domains. This compound promotes conformational changes that affect channel opening and closing, thereby influencing ion flow. Its distinct molecular architecture allows for specific electrostatic interactions, which can stabilize intermediate states of CFTR. The reaction kinetics indicate a gradual yet sustained effect on ion transport, contributing to altered cellular homeostasis.

CFTR Inhibitor II, GlyH-101

328541-79-3sc-221418
5 mg
$270.00
7
(1)

CFTR Inhibitor II, GlyH-101 is a selective inhibitor of the CFTR chloride channel, characterized by its ability to disrupt ion transport through specific allosteric modulation. This compound engages in unique hydrophobic interactions with the transmembrane domains, leading to altered channel dynamics. Its kinetic profile reveals a rapid onset of action, with a notable impact on the gating mechanisms of CFTR, ultimately affecting cellular ion balance and signaling pathways.