Drug Database
LY

lysine salicylate (lysine salicylate / Dolorosan)

✓ Approved

VUFB · Small Molecule · Small Molecule

What is lysine salicylate?

lysine salicylate is a small molecule developed by VUFB. It is approved for therapeutic indications via unknown.

Drug Profile

Brand Nameslysine salicylate, Dolorosan
CompanyVUFB
Drug ClassSmall Molecule
RouteUnknown
StatusApproved
Sources: ClinicalTrials.gov, VUFB

Therapeutic Indications

lysine salicylate is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Gastrointestinal disordersAbdominal pain✓ Approved

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PubMedCarbohydrate research2026-07-25

Enzymatic degradation of Hyaluronic acid/Poly-l-Lysine capsules for burst drug release.

Martins Luis A LA, Suesca Edward E, García-Briega María Inmaculada MI, Tatay Palmira P et al.

The aim of this study is to investigate the process by which multilayer polyelectrolyte microcapsules rupture under the action of enzymes to which the polyanion or polycation is sensitive. The capsules were prepared using a template of alginate microspheres cross-linked with calcium ions, which liquefy after the capsule has formed. The capsules are obtained via a layer-by-layer, LbL process using poly-l-lysine (PLL) as the polycation and hyaluronic acid (HA) as the polyanion. The rupture process of the capsules has been studied in media containing pronase, to which PLL is sensitive, hyaluronidase, to which HA is sensitive, or a mixture of both. The kinetics of capsule rupture are monitored by observation and counting the remaining microcapsules under a stereomicroscope or by quantifying the release of alginate into the medium. At the same time, the change in size of the microcapsules that remain intact is measured through optical microscopy, noting that the elasticity of the membrane produced by LbL allows them to swell to double their diameter before rupturing.

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PubMedThe Journal of biological chemistry2026-07-25

Histone Acetyltransferase HAT1 Regulates Intestinal Stem Cell Proliferation and Differentiation.

Nagarajan Prabakaran P, Martin Caden J CJ, Keller Andrea R AR, Akkaya-Colak Kübra B KB et al.

Stem cells are critical for the development and maintenance of tissue integrity. An important example is intestinal stem cells (ISCs) that generate all epithelial cell types necessary for formation of the intestinal lining. HAT1 is a histone acetyltransferase that acetylates newly synthesized histone H4 molecules on lysine residues 5 and 12 during replication-coupled chromatin assembly. Within the intestine, HAT1 is specifically expressed in intestinal stem and progenitor cells. We generated an inducible deletion of the HAT1 gene in intestinal epithelial cells. Following loss of HAT1, intestinal crypts became elongated, with an increase in stem and progenitor cell proliferation and an increase in the population of OLFM+ cells. Loss of HAT1 also resulted in alterations in intestinal stem cell differentiation, including an increase in the number of Goblet cells and the mislocalization of Paneth cells into villi. HAT1 is specifically responsible for the acetylation of histone H4 lysine 5 (H4K5ac) in intestinal stem cells. Genome-wide characterization of HAT1-dependent H4K5ac in intestinal crypt cells indicates that the most significant loss of H4K5ac occurs regions of the genome that correspond to in lamina-associated domains (LADs), as defined in mouse embryonic fibroblasts. Loss of H4K5ac is accompanied by an increase in histone H3 K9 tri-methylation, indicating that HAT1 regulates genome-wide histone modification patterns in intestinal crypt cells. A direct role for HAT1 in intestinal stem cell function was demonstrated using organoids in culture. HAT1 is required for differentiation in organoids and for the maintenance of Lgr5+ stem cells. These results indicate that HAT1 is required for the proper regulation of intestinal stem cell renewal and differentiation.

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PubMedInternational journal of nanomedicine2026-07-25

Protein Lactylation in Central Nervous System Diseases: Molecular Mechanisms and Targeted Therapeutic Strategies.

Cheng Ziyan Z, Ou Guangxin G, Zhang Guilong G, Ahmed Waqas W et al.

Lactate, once considered merely a metabolic byproduct, is now recognized as a cornerstone of central nervous system (CNS) homeostasis, serving as both a vital energy substrate and signaling molecule. The identification of lysine lactylation (Kla) has established this modification as a key epigenetic link between cellular metabolism and genomic regulation. This review examines the molecular mechanisms underlying protein lactylation, including enzymatic regulation by writers, erasers, and readers as well as non-enzymatic mechanisms. The multifaceted roles of Kla are explored in the context of CNS disorders, ranging from malignancies, acute injuries, and neurodegenerative diseases. The review further examines Kla's role in neuroinflammation, metabolic reprogramming, and neuroplasticity, highlighting its potential as a sensitive biomarker. Potential therapeutic strategies are also considered, including metabolic inhibitors and nanocarriers capable of crossing the blood-brain barrier (BBB) to restore metabolic and epigenetic balance.

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PubMedThe Journal of antibiotics2026-07-25

A N-methylated antimicrobial peptide targets the fructose transporter FruA of Staphylococcus aureus.

Liu Qi Q, Li Yaxuan Y, Jiang Zhichen Z, Fan Shen S et al.

Antimicrobial peptides (AMPs) represent promising alternatives to conventional antibiotics, but their therapeutic application is often hindered by suboptimal stability and poorly defined mechanisms of action. To overcome these limitations, we engineered a peptide named CAMP502NC3 through chemical modification of its parent peptide, CAMP502, which originates from marine biofilm microorganisms. The design included N-terminal acetylation, C-terminal amidation, and N-methylation of the lysine at position 3 to improve stability. CAMP502NC3 demonstrated potent activity against Staphylococcus aureus and remained stable under diverse conditions, including varying pH, high salinity, and protease exposure. Mechanistically, CAMP502NC3 leads to bacterial membrane depolarization. Transcriptomic and biochemical analyses further revealed that it interferes with key metabolic pathways, notably the fructose-specific phosphotransferase system. Molecular docking indicated direct binding of CAMP502NC3 to the fructose transporter FruA. This study illustrates how rational peptide engineering can generate stable and potent AMPs with precise membrane-associated targets, as exemplified by CAMP502NC3.

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SENP2 participates in DBP-induced oxidative stress injury via mediating Nrf2 de-SUMOylation.

Wu Xingyu X, Mao Lixin L, Jie Yang Y, Shi Xiaokai X et al.

Exposure to Di-n-butyl phthalate (DBP) is associated with congenital and acquired defects in the male reproductive system, and DBP-induced oxidative stress plays a critical role in this process. The activation of the Nrf2 antioxidant pathway plays a protective role and its ubiquitin-dependent degradation is well-established. However, the role of Nrf2 SUMOylation remains unclear. This study investigated whether the de-SUMOylating enzyme SENP2 regulates the Nrf2 pathway and mediates DBP-induced damage in Leydig cells. In both DBP-exposed rat testes and TM3 cells, SENP2 expression was significantly downregulated. Molecular assays, including Ni2+-NTA pull-down and co-immunoprecipitation (co-IP), confirmed that Nrf2 is modified by SUMO2/3 at lysine 533 and that SENP2 mediates its de-SUMOylation. Gain- and loss-of-function assays in TM3 cells showed that SENP2 knockdown activated the Nrf2 pathway, facilitated Nrf2 nuclear translocation, upregulated downstream antioxidant proteins, lowered intracellular ROS levels, and partially rescued DBP-impaired testosterone secretion. Conversely, SENP2 overexpression suppressed Nrf2 activity and nuclear translocation, and exacerbated oxidative damage and secretory dysfunction. These findings indicate that SENP2 participates in DBP-induced Leydig cell oxidative injury by modulating the de-SUMOylation of Nrf2. This study provides novel insights into the post-translational regulation of Nrf2 in environmental toxicant-induced reproductive injury, identifying the SENP2/Nrf2 axis as a potential target for intervention.

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PubMedFrontiers in nutrition2026-07-25

Process optimization and nutritional profiling of gluten-free quinoa-rice couscous: amino acid and polyphenol characterization.

El Hazzam Khadija K, Bettat Kawtar K, Metougui Mohamed Louay ML, Bazile Didier D et al.

Quinoa (Chenopodium quinoa Willd.) is internationally recognized for its exceptional nutritional profile, yet its incorporation into traditional cereal-based foods remains limited. This study developed and optimized a gluten-free couscous from quinoa and rice using D-optimal response surface methodology, evaluating the effects of quinoa fortification level (0-100%), steaming time (10-30min), and water volume (350-450 ml/kg) on techno-functional properties, proximate composition, mineral profile, bioactive compounds, and color. Quinoa fortification percentage was the dominant factor across the response set, while steaming time and water volume acted as secondary modulators. The nutritional optimum converged on 100% quinoa, with processing parameters of 20min steaming and 400 ml/kg water. Compared with commercial wheat couscous and rice-only couscous, quinoa couscous showed enhanced water-holding and oil-holding capacity, up to five-fold higher potassium, three-fold higher iron, and three-fold higher total phenolic content. LC-MS/MS amino acid putative profiling detected 18-19 of 20 amino acids in quinoa couscous versus 14 in wheat and 11 in rice couscous, with enrichment in branched-chain amino acids and detection of lysine, the limiting amino acid of cereal proteins, which was undetected in rice couscous and present only at trace levels in wheat couscous. Quinoa couscous exhibited around five-fold greater polyphenol diversity than wheat couscous, including flavan-3-ols, chalcones, and hydroxycinnamic acids exclusive to quinoa formulations. Higher quinoa levels darkened the product, with color stabilizing at fortification levels above 75%. Unlike previous work on alternative-grain couscous, this study combines process optimization with LC-MS profiling of amino acid and polyphenol composition, providing an integrated framework for gluten-free quinoa-rice couscous development. The results demonstrate that quinoa-based couscous provides a nutritionally superior, gluten-free alternative to conventional wheat couscous, with processing conditions that preserve the raw material's nutritional attributes.

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