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aztreonam lysine (Cayston / Corus 1020 / AZLI)

✓ Approved

Gilead Sciences, Inc. · Small Molecule · Small Molecule

What is aztreonam lysine?

aztreonam lysine is a small molecule developed by Gilead Sciences, Inc.. It is approved for therapeutic indications via inhaled.

Drug Profile

Brand NamesCayston, Corus 1020, AZLI
CompanyGilead Sciences, Inc.
Drug ClassSmall Molecule
RouteInhaled
StatusApproved
Sources: ClinicalTrials.gov, Gilead Sciences, Inc.

Therapeutic Indications

aztreonam lysine is developed for 3 unique indications across 2 therapeutic areas.

Therapeutic AreaConditionPhase
Infections and infestationsRespiratory tract infection✓ Approved
Infections and infestationsPneumonia pseudomonal✓ Approved
Respiratory, thoracic and mediastinal disordersBronchiectasisPhase III

Related Research Articles

PubMedFrontiers in pharmacology2026-07-17

Intraperitoneal administertion: compatibility and stability of common antibiotics in amino acid-based peritoneal dialysate.

Zhang Bohua B, Zhong Lichao L, Zhou Xueli X, Zhong Hui H et al.

The preferred method of antibiotic administration for peritoneal dialysis-related peritonitis is intraperitoneal. However, there are few studies on the compatibility of antibiotics in amino acid-based peritoneal dialysate. Our study employed High Performance Liquid Chromatography (HPLC) and amino acid analyzer to evaluate the stability of different antibiotics in amino acid-based peritoneal dialysate. We also used the two-dose method to detect the antimicrobial potency of gentamicin. Gentamicin, ciprofloxacin, heparin Sodium and fluconazole showed excellent stability under different conditions (14 days at 4 °C: ≤3.57%, 14 days at 25 °C: ≤3.77%). β-Lactam antibiotics including meropenem, ceftazidime, cefotaxime, and aztreonam showed significant degradation, especially at high temperature (37 °C)(14 days at 4 °C: ≤59.98%, 14 days at 25 °C: 19.06%-84.97%, except for aztreonam demonstrating degradation at 48 h at 37 °C (18.51%-41.88%). Among them, meropenem was the least stable (14 days at 4 °C: 59.98%, 14 days at 25 °C: 84.97%). Low concentration vancomycin is relatively stable, while medium and high concentration vancomycin has poor stability (14 days at 4 °C 500 mg/L: 45.8%, 1 g/L 27.7%). Most amino acids remained basically stable under different antibiotic environments. We counted the degradation rate of all amino acids under different conditions. The maximum degradation rate appeared on glycine, but it was only 8.21%. Finally, we also found that the antibacterial efficacy of gentamicin in acid-based peritoneal dialysate was enhanced. Most antibiotics are stable in amino acid-based peritoneal dialysate. However, β-lactams (especially meropenem, ceftazidime, and cefotaxime) and medium-to-high dose vancomycin showed significant degradation and require prompt administration. The nutritional amino acid profile in dialysate remains largely unaffected. Gentamicin demonstrates enhanced antibacterial activity in the amino acid-based peritoneal dialysate.

PMID 42465997
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PubMedJournal of the American Chemical Society2026-07-17

Redox-Active Poly(l-lysine) as a Cathode toward Sustainable Sodium-Ion Batteries.

Zhao Bowen B, Chen Chengxiang C, Yang Pan P, Huang Jinghao J et al.

The advancement of sustainable sodium-ion batteries (SIBs) necessitates cathode materials that exhibit exceptional electrochemical performance and environmentally benign end-of-life degradability. However, achieving this balance remains challenging in degradable material systems due to the intrinsic trade-off between electronic delocalization, ion transport, and structural stability. Here we report a redox-active polypeptide platform featuring a poly(l-lysine) (PLL) scaffold cross-linked with aromatic dianhydrides of varying core sizes. By enabling a "core-size modulation" strategy, this design simultaneously tunes π-conjugation and porosity, thereby coupling electronic delocalization with Na-ion transport and preserving degradability. Consequently, a poly(l-lysine)-perylenetetracarboxylic dianhydride (PLL-PTCDA or P-PT) cathode exhibits a high reversible capacity of 136.8 mAh g-1 at 50 mA g-1 and stable cycling over 15,000 cycles at 1 A g-1. Mechanistic analyses indicate that an increase in the aromatic core size promotes electronic delocalization, while enhanced porosity facilitates Na-ion transport. This combination enables reversible multielectron storage with suppressed dissolution and robust structural integrity. More importantly, the polypeptide scaffold retains intrinsic degradability, enabling chemical or enzymatic degradation once the cathode reaches its end of life. This work establishes a modular molecular-design principle that integrates electrochemical durability with programmed degradability, providing a circular pathway toward lifecycle-aware organic cathodes in next-generation sustainable SIBs.

PMID 42464459
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PubMedIn vitro cellular & developmental biology. Animal2026-07-17

Coating materials enhance urochordate primary cell culture adherence.

Qarri Andy A, Kültz Dietmar D, Gardell Alison M AM, Su Yiqun Y et al.

Marine invertebrate cell cultures are a potential source for diverse biotechnological applications, given the wide range of bioactive compounds they synthesize and accumulate. Yet, the number of established marine invertebrate cell culture systems remains limited compared with those of insects and vertebrates, particularly with respect to adherent cell cultures. Here we studied the in vitro adherence of circulating blood cells from the colonial ascidian Botryllus schlosseri. Two experimental approaches were employed, seeding blood cells either alone (setup 1) or in combination with tissue fragments (setup 2), using three basal media (DMEM, DMEM/F-12, RPMI) on culture plates coated with either Poly-L/D-lysine, gelatin, collagen, or laminin. Each experiment lasted for up to 3 d. Setup 1 results reveal that Botryllus cells remain viable and can adhere to coated surfaces in all tested media. Collagen- and laminin-coated plates supported longer-term cultures, whereas Poly-D (or L)-lysine coatings were more suitable for short-term studies. Among the basal media, RPMI and DMEM/F12 most effectively supported cell attachment. Setup 2 plates consistently showed higher cell adherence compared to setup 1, suggesting that tissue-derived factors may enhance attachment. Overall, circulating Botryllus cells demonstrate the capacity for substrate adhesion in vitro, offering a foundation for the development of adherent cell cultures.

PMID 42467177
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PubMedInternational journal of pharmaceutics2026-07-17

Lysine as a multifunctional excipient for protein-based biopharmaceutical formulations.

Lv Jia-Yi JY, Wu Shang-Yin SY, Zhang Tian-Yi TY, Fang Wei-Jie WJ

Lysine (Lys) is a nutritionally essential amino acid with a well-established parenteral safety record, yet its potential as a multifunctional excipient for protein-based biopharmaceutical formulation has not been the subject of a dedicated comprehensive review. The physicochemical properties of Lys include bifunctional amine structure, stable cationic charge under formulation relevant pH conditions, and low molecular weight suitable for free-volume anti-plasticization. These characteristics are discussed in accordance with protein formulation requirements. Thermal characterization reveals that the glass transition temperatures of frozen and dried Lys-based solids are markedly responsive to counter-ion selection, enabling rational process optimization. Stability data from liquid and freeze-dried protein systems demonstrate concentration-dependent aggregation suppression, viscosity reduction in concentrated monoclonal antibody formulations, and lyoprotective efficacy across multiple therapeutic protein classes. Four FDA-approved protein-based biologics currently incorporate Lys in their formulations. Protective mechanisms span ice nucleation inhibition, water replacement, vitrification, beta-relaxation suppression, and direct ion-dipole interactions with protein surfaces. Notably, Lys functions as an essential nutrient in upstream cell culture and as a process stabilizer throughout downstream purification, suggesting its potential applicability across multiple stages of the biopharmaceutical manufacturing lifecycle. Practical limitations including Maillard reactivity and thermal constraints are addressed. Future priorities include systematic counter-ion characterization, mechanistic studies using advanced spectroscopic methods, and integration of Lys derivatives into computationally guided formulation design.

PMID 42462918
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PubMedCell death & disease2026-07-17

SUV39H2-mediated NCOA4 methylation controls ferritinophagy and ferroptosis in triple-negative breast cancer.

Liu Lingxia L, Pei Xinyun X, Li Ding D, Huo Ying Y et al.

Triple-negative breast cancer (TNBC) exhibits iron homeostasis that supports tumor growth and proliferation, yet the regulatory mechanisms controlling iron flux remain poorly defined. Here, we identify a ferritinophagic cargo receptor NCOA4 as a novel substrate of the lysine methyltransferase SUV39H2, uncovering a previously unrecognized mechanism that regulates ferritinophagy and ferroptosis. SUV39H2 directly binds and mono-methylates NCOA4 at lysine 356, a modification that reduces NCOA4 stability. Mechanistically, K356 methylation enhances NCOA4 interaction with the E3 ligase HERC2, promoting its ubiquitination and proteasomal degradation. This degradation increases FTH1 stability, suppresses ferritinophagic flux, limits iron release, maintains the high-risk iron homeostasis and ferroptosis resistance, ultimately promoting tumor proliferation and chemoresistance. Conversely, genetic or pharmacologic inhibition of SUV39H2 (OTS186935) inhibit NCOA4 methylation, stabilizes NCOA4 protein, enhances ferritinophagy, and triggers ferroptosis. Furthermore, SUV39H2 inhibition sensitizes TNBC cells to chemotherapy in vitro and in vivo, indicating OTS186935 treatment is a feasible therapeutic strategy. Collectively, the SUV39H2-NCOA4-HERC2 axis as a critical regulatory pathway in iron metabolism and ferroptosis, and highlight inhibition of NCOA4 K356 methylation as a promising therapeutic target in TNBC.The mechanistic scheme of SUV39H2 depletion to facilitate ferroptosis in TNBC. A SUV39H2 binds and methylates NCOA4, which enhanced the interaction between NCOA4 and the E3 ubiquitin ligase HERC2, leading to NCOA4 ubiquitination and proteasomal degradation. As a result, iron metabolism was reprogramed via enhancing ferritinophagy, leading to an increase in the level of iron, ultimately triggering ferroptosis. B Cell-state transitions induced by SUV39H2.

PMID 42463647
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PubMedBritish journal of pharmacology2026-07-17

Expanding the landscape of covalent drug discovery: irreversible targeting of non-cysteine residues.

Srinivasan Bharath B, Taylor John B JB

Covalent inhibitors have re-emerged as a powerful class of therapeutics due to their prolonged target engagement, ability to decouple pharmacokinetic availability from pharmacodynamic outcome, potential for high selectivity and ability to modulate traditionally 'undruggable' targets. Historically, cysteine residues have dominated covalent drug discovery owing to their unique nucleophilicity and relative scarcity in the proteome. However, the desire to broaden the chemical scope of covalent therapeutics has driven a surge of interest in irreversibly targeting other amino acid residues, such as lysine, serine, tyrosine, threonine and histidine. This review explores the outstanding questions and challenges in developing covalent inhibitors beyond cysteine, highlighting current warhead chemistries, strategies for achieving selectivity, proteomic mapping advances, assessment of the intrinsic reactivity of the electrophiles targeting non-cysteine residues and opportunities for expanding the druggable proteome. We also discuss future directions and the pharmacological implications of non-cysteine covalent modifications in therapeutic contexts.

PMID 42464527
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