Drug Database
ES

estradiol (Vagifem)

✓ Approved

Novo Nordisk A/S · ESR1 · Small Molecule

What is estradiol?

estradiol is a small molecule developed by Novo Nordisk A/S. It is approved for therapeutic indications via intravaginal.

Drug Profile

Brand NamesVagifem
CompanyNovo Nordisk A/S
Drug ClassSmall Molecule
Molecular TargetESR1
RouteIntravaginal
StatusApproved
Sources: ClinicalTrials.gov, Novo Nordisk A/S

Mechanism of Action

Molecular Targets

estradiol acts on 1 molecular target:

ESR1estrogen receptor 1 (ER, ESR)
Want deeper analysis?Noah AI can explain complex mechanisms and compare to similar drugs.

Therapeutic Indications

estradiol is developed for 1 unique indication across 1 therapeutic area.

Therapeutic AreaConditionPhase
Reproductive system and breast disordersAtrophic vulvovaginitis✓ Approved

Related Research Articles

PubMedTherapeutic delivery2026-10-15

Process-design-translation interplay in lipid nanocarriers for vaginal mucosa delivery: how far have we advanced?

Dalabehera Manoj M

Nowadays, translational research all across the globe has increasingly been valued for focusing on mucosa delivery across the vaginal avenue, attributed to its anatomy and physiology; however, rapid mucus turnover, poor permeability, and retention popped out as the biggest constraints in this topic. Despite sidestepping these pitiable challenges, lipid nanocarriers (LNCs) are still underexplored and demand upcoming clinical demonstration to bridge the gaps between lab-human vaginal trials. Therefore, this paper delves into a process-design-translation perspective, linking vaginal barriers and lipid/excipient ratio with fabrication strategies and nanocarrier architecture. The first portion critically analyzes the key design/fabrication factors that interplay with LNCs' architecture. In the second portion, various characterization evaluation models of LNCs, viz., quality by design (QbD), lipid/excipient ratio, drug release, vaginal mucoadhesion/penetration (>10-fold higher retention), and cytotoxicity profile, have been discussed with industrial considerations and in vitro-in vivo correlation (IVIVC). Looking ahead into 5-15 years, the author suggests that hybrid LNCs, which may outperform conventional LNCs, and the integration of in-silico models could desirably enhance efficacy. Although considerable, the preclinical model doesn't outline strong enough evidence regarding optimized LNCs-vaginal mucosa delivery. A critical literature analysis was conducted through ScienceDirect, Taylor & Francis, Nature, and PubMed engines till March 2026.

PMID 42876284
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PubMedNature communications2026-10-15

Chromatin modifiers KMT2D, cBAF, and p300 cooperatively facilitate de novo binding of transcription factors on enhancers.

Van Hieu T HT, Park Young-Kwon YK, Wan Danyang D, Liu Chengyu C et al.

Transcription factors (TFs) bind to enhancers and recruit H3K4me1 methyltransferase KMT2D, chromatin remodeler cBAF, and H3K27 acetyltransferase p300 to activate transcription. However, the role of chromatin modifiers in regulating de novo binding of TFs on enhancers remains unclear. Using a robust nuclear translocation system, we show that the muscle lineage-determining TF MyoD binds to chromatin pervasively within one hour, with half of induced MyoD binding sites co-occupied by KMT2D, cBAF, and p300. On the majority of these MyoD+ enhancers, acute depletion of KMT2D or short-term inhibition of cBAF or p300 enzymatic activity markedly reduces de novo binding of MyoD as well as that of KMT2D, cBAF, and p300. On enhancers with intact MyoD binding despite these perturbations, we observe cooperative recruitment among chromatin modifiers. Similar interdependent relationships are observed between the signal-dependent TF Glucocorticoid Receptor and KMT2D, cBAF, and p300. Together, our findings show that chromatin modifiers are not only downstream effectors but also required for de novo binding of TFs on enhancers, refining a model of enhancer establishment as a process governed by functional cooperation rather than a strict hierarchy.

PMID 42875463
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PubMedNature2026-10-15

Computational design of metalloproteases.

Chen Anqi A, Wu Kejia K, Choi Hojae H, Venkatesh Preetham P et al.

De novo design of enzymes that cleave amide bonds represents a major challenge1,2. Here we use RFdiffusion methods3,4 to de novo design proteins with water-activating zinc-based active sites adjacent to a peptide substrate binding pocket. Of 135 designs tested, 36% catalyse cleavage of their cognate peptide substrates at the targeted scissile bond. The best design accelerates peptide-bond hydrolysis by more than 108-fold relative to the uncatalysed reaction; four substitutions increase this acceleration to more than 1010-fold by improving active-site preorganization5. We use this approach to design metalloproteases that selectively cleave the human disease-associated proteins TDP-43, amyloid-β and serum amyloid A, with rate enhancements of up to 109-fold. We further design caged cytokines and receptor antagonists that are selectively activated by the designed proteases, enabling bioorthogonal control of cell state. Thus, de novo design can yield highly active, programmable proteases with applications in therapeutics, biotechnology and bioremediation.

PMID 42875487
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PubMedCureus2026-10-15

Correction: Postpartum Acute Pseudo-Obstruction of the Colon (Ogilvie's Syndrome) Leading to Perforation After Spontaneous Vaginal Delivery.

Yawar Khadija K, Virk Hamza N HN, Ejaz M Sohaib MS, Rizvi Nabiha N NN et al.

[This corrects the article DOI: 10.7759/cureus.72881.].

PMID 42876858
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PubMedRenal failure2026-10-15

Acute kidney disease after acute kidney injury: incidence, risk factors, and association with de novo chronic kidney disease.

Hu Sujia S, Zhao Xingyang X, Cheng Yichun Y, Ge Shuwang S

Acute Kidney Disease (AKD) is defined as acute kidney injury (AKI) persisting for 7 to 90 days and represents a window for interventions to improve renal outcomes. However, data on AKD remain underexplored. This retrospective cohort study at Tongji Hospital, China, included 23,868 adult patients who survived at least one AKI episode between January 2015 and April 2024. Using electronic medical record data, we aimed to quantify the incidence of AKD among AKI survivors, identify independent risk factors, and evaluate the association between AKD and de novo chronic kidney disease (CKD). Among the cohort, 10,884 patients (45.6%) progressed to AKD. Multivariable logistic regression revealed that advanced age, preexisting hypertension, heart failure, cirrhosis, recent diuretic use, hepatorenal syndrome, higher baseline estimated glomerular filtration rate, higher AKI stage, and dialysis-requiring AKI were independent risk factors for AKD. Fine-Gray competing-risk analysis accounting for acute-phase mortality confirmed that higher AKI severity was independently associated with AKD progression. In a subcohort of 6597 patients without preexisting CKD who had at least one year of follow-up, 19.8% developed de novo CKD. Cox proportional hazards analysis demonstrated that patients with AKD had a significantly increased risk of de novo CKD compared to those without AKD (HR 1.92, 95% CI 1.70-2.17). These findings highlight the high proportion of AKD among patients with AKI, and emphasize the importance of early detection and targeted management for high-risk groups. It is critical to strengthen post-discharge renal function monitoring and intervention strategies for AKI patients to improve long-term renal outcomes.

PMID 42876246
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PubMedNature2026-10-15

De novo design of cysteine proteases.

Choi Hojae H, Bauer Magnus S MS, Coventry Brian B, Venkatesh Preetham P et al.

Despite advances in de novo enzyme design, success has been largely limited to low-energy-barrier model reactions. Amide bonds such as those linking amino acids along the peptide backbone are stable for hundreds of years in neutral aqueous solution because of the high energy barrier to hydrolysis1. Here we describe the de novo design of enzymes that use an activated cysteine nucleophile to hydrolyse the polypeptide backbone in a sequence-dependent manner, with a success rate of 13/69 = 19% and rate enhancements over the background reaction (kcat/kuncat) of up to 3 × 107. The designed proteases have folds that are very different from proteases in nature (TM score < 0.50), and six crystal structures are very close to the design models (Cα root mean squared deviation of <1.2 Å), highlighting the capacity for generalization and the accuracy of the design methodology. Experimental and computational analyses suggest that the remaining gap in activity to the most active native cysteine proteases arises from imperfections in active-site preorganization and substrate positioning. The designed proteases efficiently cleave their targets in mammalian cells, opening the door to a wide range of synthetic biology applications.

PMID 42875488
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