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lysine salicylate (lysine salicylate / Dolorosan)

✓ Approved

VUFB · 小分子 · 小分子

什么是 lysine salicylate？

lysine salicylate 是一种小分子，由VUFB研发。该药已获批，用于治疗相关适应症，给药途径：Unknown。

药物档案

商品名lysine salicylate, Dolorosan
公司VUFB
药物类别小分子
给药途径Unknown
状态Approved
来源： ClinicalTrials.gov, VUFB

治疗适应症

lysine salicylate 针对 1 个适应症，涉及 1 个治疗领域。

治疗领域疾病/病症分期
Gastrointestinal disordersAbdominal pain✓ Approved

相关研究文献

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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PubMedLangmuir : the ACS journal of surfaces and colloids2026-07-27

Written in Water: Hydration Repulsion Governs Selective Protein Adsorption on Saccharide Self-Assembled Monolayers.

Zhao Zhentao Z, Hayashi Tomohiro T

Saccharide-based materials are essential in bioinspired design, yet their mechanisms for resisting nonspecific protein adsorption while permitting specific binding remain unclear. This study systematically explores the relationship between surface forces and protein adsorption on glucose (Glc), lactose (Lac), and maltose (Mal) self-assembled monolayers (SAMs). Surface-sensitive techniques revealed protein resistance in the order: Mal > Lac > Glc. Among the tested proteins, bovine serum albumin (BSA) showed the lowest adsorption, immunoglobulin G (IgG) was intermediate, and fibrinogen adsorbed the most, demonstrating saccharide-dependent selectivity. Measurements revealed these surfaces generate short-range repulsive forces in physiological buffer, caused by structured interfacial water layers. The key finding is a strong link between hydration repulsion and protein adsorption behavior. The structural features of saccharides influence their interfacial water organization through hydrogen bonding, which controls resistance to nonspecific adsorption. Overall, the interfacial water acts as a dynamic barrier against protein binding. Analysis of mixed-charge residue pairs (glutamic acid-lysine and aspartic acid-lysine) on proteins, combined with potential saccharide recognition sites, suggests selective adsorption results from interplay between protein surface chemistry and interfacial hydration. This work clarifies hydration repulsion mechanisms on saccharide surfaces, establishes quantitative relationships between structure, hydration, and performance, and provides design principles for advanced biomaterials.

PMID 42503639
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PubMedJournal of cardiovascular development and disease2026-07-27

Global Profiling of Protein Lysine Lactylation in Mouse Cardiac Hypertrophy: A Lactylome Analysis.

Zhu Wengen W, Guo Siyu S, Yang Yunyao Y, Dong Yugang Y et al.

Cardiac hypertrophy, a major feature of heart failure, is closely linked to metabolic remodeling and energy deficiency. Lysine lactylation (Kla), a recently discovered post-translational modification (PTM), has been implicated in various cellular processes. However, its specific role in cardiac hypertrophy remains poorly understood. We conducted quantitative proteomics and Kla PTM analysis on left ventricular tissues from both sham-operated and aortic banding-induced hypertrophic mouse hearts. Protein samples were extracted, enriched for lactylation, and subjected to mass spectrometry. Bioinformatic analyses were performed to uncover pathways and protein-protein interactions (PPI) related to Kla-modified proteins. Our lactylome analysis identified 159 Kla-modified sites across 80 proteins, with 72 proteins exhibiting elevated Kla levels, particularly in mitochondrial and sarcomeric proteins. Pathway enrichment analysis highlighted significant involvement of fatty acid metabolism, the tricarboxylic acid (TCA) cycle, and cardiomyopathy-related pathways, underscoring the role of Kla in energy metabolism and cardiac remodeling. PPI analysis further revealed the central role of metabolic and structural proteins in the hypertrophic response. Our study provides the comprehensive analysis of Kla in cardiac hypertrophy, revealing its significant role in modulating proteins involved in mitochondrial energy metabolism and sarcomeric structure. Our findings provide a comprehensive overview of the lactylation landscape in cardiac hypertrophy and reveal extensive lactylation changes in proteins associated with mitochondrial metabolism and sarcomeric organization. These observations suggest a potential link between Kla and cardiac hypertrophy, which warrants further functional investigation.

PMID 42505874
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PubMedJournal of agricultural and food chemistry2026-07-27

Histone H3K36 Methyltransferase MaSET40 Regulates Cold Tolerance in Banana Fruit.

Yang Hui H, Zhou Yijie Y, Li Ying Y, Liang Hanzhi H et al.

Histone methylation is an important epigenetic mechanism that regulates plant development and stress responses, but its role in postharvest fruit chilling injury remains unknown. Here, we identified a cold-inducible SET domain protein, MaSET40, in banana (Musa acuminata) and found that it functions as a trimethylation of histone H3 lysine 36 (H3K36me3) methyltransferase. Transient overexpression of MaSET40 in banana fruit peel accelerated chilling injury, whereas virus-induced silencing of MaSET40 alleviated cold-induced peel damage. Transcriptome profiling revealed that MaSET40 activates genes involved in reactive oxygen species (ROS) accumulation and membrane lipid degradation, including MaPPO1, MaPPO3, MaRBOHB, Malipase, MaPLA2, and MaLOX3.1. Chromatin immunoprecipitation followed by quantitative PCR (ChIP-qPCR) further showed that MaSET40 increased H3K36me3 enrichment at these gene loci, accompanied by higher transcript levels. These results reveal an H3K36me3-mediated epigenetic mechanism that promotes chilling injury in postharvest banana fruit and identify MaSET40 as a potential target for improving cold tolerance in tropical fruits.

PMID 42503791
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PubMedJournal of the American Chemical Society2026-07-27

Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron Oxidative Enzyme during RiPP Biosynthesis.

Hebron Dayna P DP, Shriver Tucker J TJ, Ziarek Joshua J JJ, Rosenzweig Amy C AC

Ribosomally synthesized and post-translationally modified peptides (RiPPs) are produced by biosynthetic enzymes that modify genetically encoded precursor peptide backbones and side chains. Genome mining and bioinformatics analyses targeting the multinuclear nonheme iron oxidative (MNIO) enzyme family led to the identification of a RiPP biosynthetic gene cluster from Streptomyces thermodiastaticus JCM 4840, the std cluster, which includes multiple biosynthetic enzymes and a precursor peptide containing a conserved SNKEWQE motif. Using in vitro approaches, we elucidated the modifications installed by the std biosynthetic enzymes. First, a YcaO-TfuA pair thioamidates the asparagine backbone. Next, a peptidase with an S8/S53 domain fused to a NodU-like carbamoyltransferase both carbamoylates the ε-amino group of lysine to produce the nonproteinogenic amino acid homocitrulline and cleaves the C-terminal EWQE motif. Finally, a partner protein-MNIO pair bis-hydroxylates the β- and γ-carbon positions of the installed homocitrulline to create dihydroxyhomocitrulline. The formation of homocitrulline and dihydroxyhomocitrulline is unprecedented in RiPP biosynthesis. Moreover, these findings expand the known substrate scope of YcaO-TfuA enzymes and MNIOs and identify new roles for carbamoyltransferases in these pathways.

PMID 42503680
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