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carbocysteine lysine salt (Fluifort / Pectox Lisina)

✓ Approved

Dompe · Small Molecule · Small Molecule

What is carbocysteine lysine salt?

carbocysteine lysine salt is a small molecule developed by Dompe. It is approved for therapeutic indications via oral (po).

Drug Profile

Brand NamesFluifort, Pectox Lisina
CompanyDompe
Drug ClassSmall Molecule
RouteOral (PO)
StatusApproved
Sources: ClinicalTrials.gov, Dompe

Therapeutic Indications

carbocysteine lysine salt is developed for 2 unique indications across 2 therapeutic areas.

Therapeutic AreaConditionPhase
Congenital, familial and genetic disordersCystic fibrosis✓ Approved
Respiratory, thoracic and mediastinal disordersBronchitis chronicPhase I

Related Research Articles

PubMedPhysical chemistry chemical physics : PCCP2026-11-12

Deciphering the role of lysine mutation in the stability and dynamics of the Cren7-DNA complex.

Verma Arunima A, Mondal Padmabati P

Cren7, a conserved chromatin protein in Crenarchaeota, organizes and stabilizes genomic DNA. The chromatin protein Cren7 plays a key role in maintaining DNA architecture and stability in hyperthermophilic archaea. Its interaction with DNA is largely mediated by positively charged lysine residues that establish strong electrostatic and hydrogen-bond interactions with the negatively charged phosphate backbone. In this study, we investigated how lysine mutations affect the structural stability and dynamics of the Cren7-DNA complex using all-atom molecular dynamics simulations. Comparative analyses between the wild-type and lysine-to-alanine mutants revealed noticeable perturbations in the DNA stability as well as complex stability via the protein-DNA interface. These results reflect the importance of lysine residues, with Lys48, Lys53, and Lys24 having the highest impact on the Cren7-DNA stability. Furthermore, this study demonstrates that the differential effects of lysine mutations on DNA stability in the Cren7-DNA complex not only depend on the position of the mutated residue in the same Cren7 but also reflect the combined effects of the protein position, DNA sequence, and coupling.

PMID 43016212
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PubMedJournal of medicinal chemistry2026-11-12

Alkyl-Branched Acyl-Lysine Peptides as Potent Cell-Permeable Slow-Substrate Inhibitors of SIRT2.

Friedrich Florian F, Meleshin Marat M, Kalbas Diana D, Kollmer Franziska F et al.

Sirtuin 2 (SIRT2) is a nicotinamide adenine dinucleotide (NAD+)-dependent lysine deacylase implicated in cancer and neurodegeneration. Here, we report acyl-lysine peptide inhibitors bearing methyl-branched or cyclopropyl-modified acyl chains with low-nanomolar inhibitory potency. Their prolonged residence time and minimal catalytic turnover, confirmed by kinetic analysis, support a "slow substrate" inhibition mechanism. Ternary crystal structures of SIRT2-peptide-NAD+ complexes are consistent with a rate-limiting initial nucleophilic attack of the amide oxygen on NAD+. The inhibitors stabilize a catalytically competent yet unproductive enzyme state, distinct from thiocarbonyl inhibitors that form stalled intermediates with NAD+. Comparative structural and biochemical analyses with SIRT1 and SIRT3 reveal isoform-specific acyl chain trajectories underlying selectivity. Extension to potentially naturally occurring or drug-derived Nε-lysine modifications, i.e., phytanoyl- and ibuprofenyl-lysine, demonstrates that diverse branched acyl groups inhibit SIRT2. In cells, optimized inhibitors show low-nanomolar target engagement and induce robust α-tubulin hyperacetylation, establishing slow substrate inhibition as a strategy for selective sirtuin targeting.

PMID 43018589
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PubMedCell death & disease2026-11-12

YAP delactylation enhances therapy resistance in renal cell carcinoma.

Lin Mingjie M, Jin Xiaohan X, Chen Minyu M, Fu Liangmin L et al.

Lactylation is a novel lysine acylation modification, and its function and exact mechanisms remain unclear. The responsiveness to combined targeted and immunotherapy continues to be a major challenge in cancer treatment. Here, we discovered that lysine lactylation (Kla) is specifically downregulated in targeted therapy-resistant renal cancer cells and tissues. The lactylation status of YAP at lysine 90 (K90) regulates its nuclear translocation, which is critical for the expression of epithelial-mesenchymal transition (EMT)-related genes and the PD-L1 gene. Furthermore, we identified HDAC1 as the "eraser" of YAP-K90 lactylation. By transfecting YAP-K90T (a lactylation mimic), we enhanced antitumor immune activity. In xenograft models established in huCD34+HSC NCG mice, we consistently found that HDAC1 inhibition enhances the response to combination therapy by increasing YAP lactylation and promoting CD8⁺ T cell tumor infiltration. These findings reveal lactylation as a key mechanism in targeted drug response and identify inhibiting YAP delactylation as a promising strategy for renal cell carcinoma treatment.

PMID 43015268
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PubMedDermatology and therapy2026-11-12

Forty-Eight-Week Real-World Outcomes of Ritlecitinib in Alopecia Areata: Delayed Responses and Predictive Value of Change in SALT Score at Week 24.

Kuwabiraki Hiroto H, Imanishi Hisayoshi H, Watanabe Miki M, Imanishi Akiko A et al.

Alopecia areata (AA) is an autoimmune disease characterized by non-scarring hair loss. Although ritlecitinib has demonstrated efficacy in moderate-to-severe AA, real-world data on 48-week outcomes and predictors of longer-term response remain limited. We conducted a retrospective, single-center, observational study of 41 patients with moderate-to-severe AA who received ritlecitinib (50 mg/day) at Osaka Metropolitan University Hospital, Japan. Effectiveness and safety were evaluated for up to 48 weeks. Patients evaluable at week 48 were classified as responders (Severity of Alopecia Tool [SALT] score ≤ 20) or non-responders (SALT score > 20). The predictive value of the change in SALT score from baseline (ΔSALT) for response at week 48 was assessed using receiver operating characteristic (ROC) analysis. At week 48, 39.3% (11/28) and 35.7% (10/28) of patients achieved SALT scores ≤ 20 and ≤ 10, respectively. Responders at week 48 (week-48 responders) showed greater improvement in ΔSALT at week 24 (week-24 ΔSALT) than non-responders (median: - 50.0 vs. 0.0; P = 0.006). Of the 21 patients who had not achieved a SALT score ≤ 20 at week 24, five subsequently achieved this outcome at week 48. ROC analysis showed that week-24 ΔSALT had predictive value for week-48 response (area under the curve [AUC] 0.81; 95% confidence interval 0.619-1.000), with a cutoff of - 40 yielding 81.8% sensitivity and 88.2% specificity. Two patients (4.9%) discontinued ritlecitinib because of adverse events; all other adverse events were mild and did not require treatment discontinuation. Ritlecitinib showed real-world effectiveness through 48 weeks in patients with moderate-to-severe AA. Delayed responses beyond week 24 were observed, and week-24 ΔSALT may have potential value in predicting response at week 48, although these findings require validation in larger cohorts.

PMID 43015456
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PubMedThe journal of physical chemistry. B2026-11-12

Harnessing Hofmeister Salt Effects for Confined Photosensitized Oxidation in a Porphyrin-Based Supramolecular Nanoreactor.

Liu Xuan X, Kang Zhicheng Z, He Hui H, Tang Jiadong J et al.

Coexisting inorganic ions and multiple water-soluble organic dyes in saline wastewater often compromise substrate selectivity and photosensitized efficiency, creating challenges for effective pollutant dye removal. To overcome these limitations, we developed a heterogeneous supramolecular photosensitized system based on a microporous porphyrin organic cage (HP3C) and investigated its size-selective photosensitized behavior toward water-soluble dyes, together with the salt-regulated confined enrichment effect. Photophysical studies revealed that HP3C efficiently generated reactive oxygen species (ROS) under light irradiation, including singlet oxygen (1O2) and superoxide radicals (O2•-). Under 440-445 nm light irradiation, HP3C exhibited molecular-size-dependent photosensitization. Indigo carmine (IC), with molecular dimensions compatible with the cage cavity, achieved rapid decolorization within 10 min with a rate constant of 0.336 min-1, which is approximately 20-fold higher than those of geometrically mismatched dyes. Notably, the presence of salts, particularly Na2SO4, further enhanced IC decolorization with the rate constant increasing to 0.514 min-1, an approximately 1.5-fold enhancement over the salt-free system. Hofmeister analysis and DFT calculations suggest that salting-out-induced dehydration promoted IC enrichment toward the hydrophobic cage of HP3C, enabling confined oxidation through shortened substrate-ROS diffusion pathways. This work establishes a salt-assisted confined photosensitization strategy for selective decolorization of water-soluble dye pollutants in saline environments.

PMID 43018306
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PubMedmBio2026-11-12

Host-mediated SUMOylation of pE248R promotes African swine fever virus replication and virulence.

Li Dan D, Ren Jingjing J, Wu Junhuang J, Zhu Guoqiang G et al.

SUMOylation, the covalent conjugation of small ubiquitin-like modifier (SUMO) proteins to lysine residues in target substrates, is an essential post-translational modification in eukaryotes. Recently, microbial manipulation of SUMOylation has emerged as an important virulence strategy for viruses. Here, we demonstrate that African swine fever virus CN/GS/2018 (ASFV CN/GS/2018) pE248R can be conjugated to SUMO1 and provide evidence that prevention of pE248R SUMOylation can block ASFV CN/GS/2018 infection. The E3 SUMO ligase PIAS4 interacts with pE248R via its SUMO interaction motifs (SIMs) and promotes pE248R SUMOylation at its lysine residues at positions 103 and 240. Additionally, PIAS4 can increase the stability of pE248R. Importantly, studies on ASFV CN/GS/2018 pE248R with mutations have shown that the SUMOylation sites, the SIMs, or both are essential for the viral replication cycle in vitro and that mutations in these regions attenuate the virus in swine. Collectively, these findings indicate that ASFV CN/GS/2018 pE248R SUMOylation is critical for ASFV CN/GS/2018 pathogenesis and virulence, thereby providing a potential strategy for ASF vaccine development.IMPORTANCEAfrican swine fever virus (ASFV) poses a devastating threat to the global swine industry, yet effective vaccines and antiviral strategies remain unavailable. While microbial manipulation of host post-translational modifications is a common virulence strategy, how ASFV exploits the host SUMOylation machinery has remained elusive. Here, we demonstrate that ASFV CN/GS/2018 pE248R undergoes SUMO1 conjugation mediated by the E3 SUMO ligase PIAS4 via specific SUMO-interacting motifs, which enhances pE248R stability and is essential for the viral replication cycle and virulence in swine. Blocking pE248R SUMOylation at lysine residues 103 and 240 inhibits viral infection, revealing that ASFV CN/GS/2018 hijacks the host SUMOylation system as a critical pathogenesis mechanism. These findings identify a druggable virus-host interaction node and provide a rational target for developing next-generation attenuated ASFV vaccines.

PMID 43018350
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