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

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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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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PubMedJournal of medicinal chemistry2026-11-12

Discovery of Novel Quinazoline-Based KDM1A Inhibitors as Dual Inducers of Ferroptosis and Apoptosis in Esophageal Cancer.

Zhao Li-Juan LJ, Yu Rui R, Liu Ying Y, Yin Jia-Yi JY et al.

Lysine-specific demethylase 1 (KDM1A) is an FAD-dependent epigenetic target implicated in cancer progression. Starting from lead compound ZY-1 (IC50 = 105 nM), we designed a series of quinazoline-based reversible KDM1A inhibitors via a functional group migration strategy. Structure-activity relationship studies (SARs) identified JH-1 as the most potent analogue, with an IC50 of 35 nM. JH-1 selectively binds KDM1A, inhibits H3K4me1/2 demethylation, and induces both ferroptosis (lipid ROS accumulation) and apoptosis in esophageal cancer cells. In a KYSE510 xenograft model, oral administration of JH-1 significantly suppressed tumor growth without obvious toxicity. These results establish JH-1 as a promising reversible KDM1A inhibitor and validate the quinazoline scaffold for epigenetic cancer therapy.

PMID 43018546
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PubMedCell death discovery2026-11-12

Levistilide A promotes ferroptosis through the RNF40-HSP90α axis and inhibit colorectal cancer lung metastasis.

He Jia-Ming JM, Li Chang-Shuo CS, Liu Ying-Qian YQ, Wei Qiang Q et al.

The molecular mechanisms underlying lung metastasis of colorectal cancer (CRC) remain largely elusive, and effective therapeutic agents are still lacking. In this study, we identify levistilide A (LeA) as a potential anti-metastatic agent against CRC lung metastasis. We demonstrate that heat shock protein 90α (HSP90α) is markedly upregulated in CRC and promotes lung metastasis by suppressing ferroptosis. Notably, combined treatment with LeA and the ferroptosis inducer RSL3 further alleviates lung metastatic burden in vivo. Mechanistically, we reveal that the E3 ubiquitin ligase ring finger protein 40 (RNF40) suppresses CRC cell proliferation by directly interacting with HSP90α, inducing ubiquitination at lysine 407 and promoting its proteasomal degradation. RNF40-mediated HSP90α downregulation leads to the accumulation of malondialdehyde (MDA) and reactive oxygen species (ROS), thereby inhibiting CRC cell growth. Collectively, our findings provide mechanistic insights into how LeA directly targets HSP90α or facilitates RNF40-HSP90α-mediated degradation of HSP90α to regulate ferroptosis in CRC.

PMID 43015276
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