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aztreonam lysine (Cayston / Corus 1020 / AZLI)

✓ Approved

Gilead Sciences, Inc. · 小分子 · 小分子

什么是 aztreonam lysine？

aztreonam lysine 是一种小分子，由Gilead Sciences, Inc.研发。该药已获批，用于治疗相关适应症，给药途径：Inhaled。

药物档案

商品名Cayston, Corus 1020, AZLI
公司Gilead Sciences, Inc.
药物类别小分子
给药途径Inhaled
状态Approved
来源： ClinicalTrials.gov, Gilead Sciences, Inc.

治疗适应症

aztreonam lysine 针对 3 个适应症，涉及 2 个治疗领域。

治疗领域疾病/病症分期
Infections and infestationsRespiratory tract infection✓ Approved
Infections and infestationsPneumonia pseudomonal✓ Approved
Respiratory, thoracic and mediastinal disordersBronchiectasisPhase III

相关研究文献

PubMedThe new microbiologica2026-07-27

In Vitro Susceptibility of Ceftazidime-Avibactam- Resistant Klebsiella pneumoniae Isolates to the Ceftazidime-Avibactam Plus Aztreonam Combination Using the Broth Disk Elution Method.

Karpuz Tuncer T, Koyuncu Özyurt Özlem Ö, Yazısız Hatice H, Öngüt Gözde G et al.

Infections caused by multidrug-resistant Gram-negative bacteria, particularly carbapenemase-producing Enterobacterales, present significant diagnostic and therapeutic challenges, highlighting the need for practical laboratory methods to evaluate combination therapies. This study investigated 90 ceftazidime-avibactam (CZA)-resistant Klebsiella pneumoniae isolates collected from clinical specimens between January 2021 and July 2023. Species identification was performed using MALDI-TOF MS, and antimicrobial susceptibility testing was conducted with the BD Phoenix™ system according to Clinical and Laboratory Standards Institute (CLSI) criteria, with disk diffusion used for confirmation when necessary. Carbapenemase production was determined phenotypically using the modified Carbapenem Inactivation Method. For a subset of isolates with available whole-genome sequencing data, resistance genes were confirmed, although genotypic analysis was not performed for all isolates. The in vitro activity of the CZA plus aztreonam (CZA-ATM) combination was evaluated using the CLSI-recommended broth disk elution method. All isolates were resistant to CZA and aztreonam when tested individually, whereas no visible growth was observed with the combination, indicating in vitro susceptibility. These findings suggest that the broth disk elution method is a practical approach for assessing CZA-ATM activity in routine clinical laboratories. Further studies including reference method validation and evaluation of borderline or resistant isolates are needed.

PMID 42507122
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PubMedAntibiotics (Basel, Switzerland)2026-07-27

Physicochemical Stability of Aztreonam/Avibactam in Elastomeric Devices for Outpatient Parenteral Antimicrobial Therapy.

Toro Blanch Cristina C, Larrea Urtaran Xabier X, Aguilar Salmerón Raquel R, Prat Riera Alba A et al.

Outpatient Parenteral Antimicrobial Therapy (OPAT) programs provide a safe and cost-effective strategy for administering intravenous antimicrobials in the home setting. Aztreonam/avibactam (ATM/AVI) is a reserve antibiotic used to treat infections caused by multidrug-resistant Gram-negative bacteria. The aim of this study was to evaluate the physicochemical stability of ATM/AVI in elastomeric pumps for OPAT use. ATM/AVI was diluted in a 0.9% sodium chloride solution to a concentration of 25/8.33 mg/mL and stored in elastomeric pumps (Infusor LV 10 mL/h, 240 mL; Baxter Healthcare S.A, Zurich, Switzerland). The devices were maintained at 4 °C for 14 days and at 25, 32, and 37 °C for 48 h. Three independent elastomeric devices were prepared for each temperature condition and sampled in duplicate at each time point. Solutions were considered stable if the color, clarity, and pH remained unchanged and if the percentage of intact drug remained ≥90%, as determined via UHPLC-MS/MS. ATM/AVI in polyisoprene elastomeric devices remained physicochemically stable for up to 14 days under refrigerated conditions and for 48 h at 25 °C, 32 °C, and 37 °C. ATM/AVI solutions demonstrated prolonged stability under the evaluated conditions, supporting their potential use in OPAT programs via 24 h continuous infusion.

PMID 42505671
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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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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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