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carbocysteine lysine salt (Fluifort / Pectox Lisina)

✓ Approved

Dompe · 小分子 · 小分子

什么是 carbocysteine lysine salt？

carbocysteine lysine salt 是一种小分子，由Dompe研发。该药已获批，用于治疗相关适应症，给药途径：Oral (PO)。

药物档案

商品名Fluifort, Pectox Lisina
公司Dompe
药物类别小分子
给药途径Oral (PO)
状态Approved
来源： ClinicalTrials.gov, Dompe

治疗适应症

carbocysteine lysine salt 针对 2 个适应症，涉及 2 个治疗领域。

治疗领域疾病/病症分期
Congenital, familial and genetic disordersCystic fibrosis✓ Approved
Respiratory, thoracic and mediastinal disordersBronchitis chronicPhase I

相关研究文献

PubMedPlant cell reports2026-07-27

ABI5-activated ALKBH10B demethylates RAP2.6 mRNA to modulate Arabidopsis salt tolerance.

Xuan Shurong S, Cheng Mengxue M, Wen Yunze Y, Wei Qiang Q et al.

Salt stress induces ABI5 → ALKBH10B transcription; the demethylase removes m6A from RAP2.6 mRNA, accelerating its decay and attenuating salt-responsive genes, thus linking ABA signaling to reversible m6A control of Arabidopsis salt tolerance. N6-methyladenosine (m6A) is the most prevalent internal modification of RNA and plays an important role in regulating RNA metabolism that governs development and environmental adaptation of plants. Here we dissect how the Arabidopsis m6A demethylase ALKBH10B is integrated into abscisic-acid (ABA)-mediated salt-stress signaling. Under salt treatment, loss of ALKBH10B exhibited significantly delayed seed germination. Salt stress could significantly induce the expression of ALKBH10B transcription via the ABA-responsive transcription factor ABI5, which binds directly bind to the ABRE element in the ALKBH10B promoter and activate its transcription. Multi-omic integration of m6A methylomes and transcriptome identified the AP2/ERF transcription factor RAP2.6 as a direct target of ALKBH10B. ALKBH10B removed m6A modifications on RAP2.6 mRNA, accelerating its degradation and modulating the expression of salt-responsive genes. In summary, this study elucidates the salt stress response pathway ABI5-ALKBH10B-RAP2.6 that couples ABA perception to reversible m6A modification, providing mechanistic insight into the intricate regulatory network of dynamic m6A modifications in plant stress adaptation.

PMID 42507133
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PubMedZhonghua yu fang yi xue za zhi [Chinese journal of preventive medicine]2026-07-27

[Application progress of implementation research on salt reduction strategies].

Sun Y T YT, Hu Y M YM, Wei D W DW, Li M S MS et al.

Based on the high global average salt intake among adults, the implementation of salt reduction strategies-as a key measure for preventing and controlling non-communicable diseases such as hypertension-faces significant challenges in translating scientific evidence into practice. Implementation research has emerged as a crucial methodological approach to facilitate this translation by systematically analyzing the facilitators and barriers associated with salt reduction interventions. This review summarizes the research content and major progress in implementation research on salt reduction strategies both domestically and internationally, aiming to provide a reference for future implementation studies.

PMID 42503944
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PubMedJournal of experimental botany2026-07-27

PHYTOCHROME-INTERACTING FACTOR 3 represses plant salt tolerance through MADS-box transcription factor AGAMOUS-LIKE 21.

Zhang Yiyi Y, Feng Xixian X, Liu Zhongping Z, Xing Shiqi S et al.

Salt stress poses a threat to plant water and nutrient uptake and leads to multiple forms of damages in plants, making it a major challenge to global crop production. PHYTOCHROME-INTERACTING FACTOR 3 (PIF3) is a key transcription factor in light signaling and it has been reported to play a critical role in plant responses to salt stress. Here, we demonstrated that PIF3 negatively regulates plant salt tolerance in Arabidopsis, and salt stress significantly enhances the interaction between PIF3 and light-activated PHYTOCHROME B (PHYB), leading to accelerated degradation of PIF3 in light, thus alleviating its negative regulation on plant salt tolerance. Additionally, we identified AGAMOUS-LIKE 21 (AGL21) as a downstream target gene of PIF3. PIF3 directly binds to the promoter of the AGL21 gene to promote its expression. The PIF3-AGL21 module transcriptionally modulates the expression a battery of downstream genes, including those involved in redox homeostasis regulation, thereby leading to accumulation of reactive oxygen species (ROS) and disruption of redox homeostasis within plants in response to salt stress. PHYB-mediated degradation of PIF3 attenuates the PIF3-AGL21 module to restore redox homeostasis and enhance plant tolerance to salt stress.

PMID 42504752
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PubMedGels (Basel, Switzerland)2026-07-27

Development and Performance Evaluation of a High-Temperature-Resistant Salt-Responsive Micro-Crosslinked Polymer Gel Filtration Loss Reducer.

Xiao Fengfeng F, Xia Yuhao Y, Liu Wushuo W, Liu Jingping J et al.

To address the difficulty in controlling the filtration performance of water-based drilling fluids under high-temperature and high-salinity conditions during the drilling of deep and ultra-deep wells, a salt-responsive micro-crosslinked polymer gel filtration loss reducer, designated LZX, was developed. The synthesis employed 2-acrylamido-2-methylpropane sulfonic acid (AMPS), N,N-dimethylacrylamide (DMAA), dimethyldiallylammonium chloride (DMDAAC), and a betaine monomer containing an unsaturated double bond as monomers, with polyethylene glycol diacrylate (PEGDA) introduced as a crosslinker. Experimental results showed that the product structure matched the design expectations, and the thermal decomposition temperature of the main molecular chain exceeded 290 °C, indicating good thermal stability. At 220 °C under saturated salt conditions, a dosage of 2.5 wt% LZX maintained the API filtration loss at 5.8 mL and the HPHT filtration loss at 28.6 mL. Comparative experiments at different temperatures demonstrated that LZX exhibited superior filtration control performance compared to the commercial high-temperature filtration reducer Driscal Temp and Driscal D. The micro-crosslinked structure of LZX enhanced the rigidity of the molecular chains, raising the upper limit of its thermal resistance. Rheological and viscosity-average molecular weight measurements revealed that LZX exhibited typical antipolyelectrolyte behavior in high-salinity environments-the molecular chains tended to extend and the filtration reduction capability was accordingly maintained-preliminarily achieving a functional transition from passive salt tolerance to active salt responsiveness. LZX is expected to support the construction of high-performance water-based drilling fluids with high temperature and high salt resistance for future deep-earth drilling.

PMID 42505248
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PubMedMolecular pharmaceutics2026-07-27

Intracellular Delivery of Full-Length Antibodies via Poly-l-lysine-Coated PEG-PLGA Polymersomes Enables Noninvasive Pulmonary Immunotherapy.

Nazar Vida V, Buxton Lincoln Paul LP, Jiang Sui S, Culick Allison Irene AI et al.

The intracellular delivery of full-length antibodies offers substantial therapeutic potential but remains limited by poor cellular uptake, extracellular degradation, and inefficient encapsulation strategies. Here, we report a noninvasive, scalable, and biocompatible nanocarrier platform based on poly-l-lysine (PLL)-coated polyethylene glycol-block-poly(lactic-co-glycolic acid) (PEG-PLGA) polymersomes for efficient intracellular antibody delivery. Coating polymersomes with 30 kDa ε-poly-l-lysine increased antibody encapsulation efficiency to ∼ 80%. It enabled precise modulation of surface charge to a mildly positive ζ-potential (∼+4.5 mV), while maintaining nanoscale dimensions (hydrodynamic diameter ≈ 420 ± 30 nm). The resulting formulation exhibited excellent biocompatibility, preserving >96% cell viability in primary human pulmonary fibroblasts. Importantly, PLL-coated polymersomes facilitated efficient intracellular delivery of full-length antibodies and preserved their biological function, as demonstrated by robust suppression of NOD-like receptor family pyrin domain-containing 3 (NLRP3)-dependent IL-1β signaling. Upon pulmonary administration via aerosolization, polymersomes delivered the antibody efficiently to lung-resident cells in vivo without detectable acute cytotoxicity. To our knowledge, this work represents the first demonstration of PLL-coated PEG-PLGA polymersomes enabling intracellular delivery of full-length antibodies both in vitro and in vivo, establishing a versatile nanoplatform for lung-targeted intracellular antibody therapeutics.

PMID 42503719
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PubMedJournal of bacteriology2026-07-27

Identification of a conserved GNAT-family lysine acetyltransferase in Streptococcus gordonii involved in biofilm formation and oral colonization.

O'Brien Joseph J, Saavedra Flavia M FM, Choi Irene I, McCulloch Kyle J KJ et al.

Streptococcus gordonii is a gram-positive oral bacterium capable of adhering to a variety of biotic and abiotic surfaces and forming biofilms. To characterize physiological changes associated with biofilm formation in S. gordonii, we investigated the roles of two putative GCN5-related N-acetyltransferases (GNATs), SGO_2030 and SGO_2031, in in vitro biofilm formation on saliva-coated surfaces using the laboratory strain DL1. Our results demonstrate that SGO_2031, but not SGO_2030, seems to contribute to biofilm formation by modulating the abundance of extracellular polysaccharides within the biofilm matrix. This defect in biofilm formation observed by the deletion of SGO_2031 resulted in a significant fitness disadvantage during colonization of the murine oral cavity compared to the wild-type parent strain. Consistent with the role of S. gordonii as an early colonizer of tooth surfaces that influences oral biofilm community structure, inoculation with either the wild-type or the SGO_2031 mutant strain led to distinct alterations in the murine oral microbiome composition. Deletion of SGO_2031 also resulted in changes in protein acetylation patterns, as assessed by Western immunoblot analysis, supporting the role of this enzyme as an acetyltransferase. Given that SGO_2031 is conserved and widely distributed among streptococci, we propose naming this enzyme Streptococcal Lysine Acetyltransferase A (SktA). Protein acetylation is a common posttranslational modification conserved across all domains of life. In bacteria, protein acetylation is carried out by homologs of the GCN5-related N-acetyltransferase (GNAT) family. GNATs catalyze the transfer of an acetyl group from acetyl-CoA to the ε-amino group of lysine residues on proteins. This process changes the charge and length of lysine residues, resulting in changes to protein function. Streptococcus gordonii is predicted to encode 17 GNAT homologs. Here, we report that one of them, SGO_2031 (SktA), plays an important role in S. gordonii biofilms.

PMID 42506740
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