ArticlePloS one2014
Protonated form: the potent form of potassium-competitive acid blockers.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Protonation of Key Acidic Residues Reveals Binding Features of PCABs to Gastric H, K-ATPase.The Journal of membrane biology · 2026Article
- Vonoprazan-amoxicillin dual regimen withWorld journal of gastroenterology · 2024Article
- Gastroprotective effect of rhodanine and 2,4-thiazolidinediones scaffolds in rat stomachs by contribution of anti-apoptotic (BCL-2) and tumor suppressor (P53) proteins.Scientific reports · 2024Article
- Current research status and trends of potassium-competitive acid blockers in the treatment of acid-related diseases: a bibliometric analysis.Frontiers in pharmacology · 2024Article
- Predicting pharmacodynamic effects through early drug discovery with artificial intelligence-physiologically based pharmacokinetic (AI-PBPK) modelling.Frontiers in pharmacology · 2024Article
- Review of recent evidence on the management of heartburn in pregnant and breastfeeding women.BMC gastroenterology · 2022Review
- The binding selectivity of vonoprazan (TAK-438) to the gastric H+, K+ -ATPase.Alimentary pharmacology & therapeutics · 2015Article
- Vonoprazan: first global approval.Drugs · 2015Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Potassium-competitive acid blockers (P-CABs) are highly safe and active drugs targeting H+,K+-ATPase to cure acid-related gastric diseases. In this study, we for the first time investigate the interaction mechanism between the protonated form of P-CABs and human H+,K+-ATPase using homology modeling, molecular docking, molecular dynamics and binding free energy calculation methods. The results explain why P-CABs have higher activities with higher pKa values or at lower pH. With positive charge, the protonated forms of P-CABs have more competitive advantage to block potassium ion into luminal channel and to bind with H+,K+-ATPase via electrostatic interactions. The binding affinity of the protonated form is more favorable than that of the neutral P-CABs. In particular, Asp139 should be a very important binding site for the protonated form of P-CABs through hydrogen bonds and electrostatic interactions. These findings could promote the rational design of novel P-CABs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.