pe
pep-04426 v1 CC-BY-SA-4.0

Bivalirudin: Angiomax/Angiox blood-clot preventer used during heart procedures

A lab-made protein given through an IV during artery-opening heart procedures (stenting) to stop dangerous clots from forming; also the go-to option when patients can't take heparin because of an immune reaction that causes clotting. FDA-approved drug.

statusbioassayed target? length20 aa refs30
fda-approved
status 5 / 5
sequence20 aa
15101520
FPRPGGGGNGDFEEIPEEYL
overview readme

What this is

Bivalirudin (brand name Angiomax in the US, Angiox in Europe) is a 20-amino-acid synthetic peptide given by intravenous infusion as an anticoagulant during percutaneous coronary intervention (PCI) — the cardiac catheterization procedure that opens a blocked coronary artery, usually with a stent. It blocks thrombin, the central enzyme of clot formation, by binding two separate sites on the thrombin molecule at the same time. It is also the standard alternative anticoagulant for patients who cannot receive heparin because of heparin-induced thrombocytopenia (HIT) — an immune reaction in which heparin paradoxically triggers clotting and a drop in platelets (Warkentin 2005; Lee 2011). The molecule was designed as a short, reversible mimic of hirudin, the natural anticoagulant from the saliva of the medicinal leech, and its N-terminal residue is D-phenylalanine (encoded as the standard letter "F" in the stored 20-letter sequence) — a non-natural D-amino acid that protects the active-site contact from rapid proteolysis (Gladwell 2002).

History

Bivalirudin was designed at Biogen in the early 1990s under the development name Hirulog (later BG8967) as part of a structure-guided program to engineer a small, synthetic peptide that retained hirudin's bivalent grip on thrombin while being chemically tractable and dosable. The drug was eventually licensed to The Medicines Company and approved by the US FDA in December 2000 under the brand name Angiomax, initially for anticoagulation in patients with unstable angina undergoing percutaneous transluminal coronary angioplasty. The label was subsequently expanded to cover PCI more broadly, including patients with or at risk of HIT (Deeks 2008). The modern evidence base was then built by a sequence of large randomized trials in interventional cardiology: REPLACE-2 in elective and urgent PCI (Lincoff 2003, JAMA), ACUITY in acute coronary syndromes (Stone 2006, NEJM), HORIZONS-AMI in primary PCI for ST-elevation myocardial infarction (Stone 2008, NEJM), EUROMAX for ambulance-initiated anticoagulation in STEMI (Steg 2013; Zeymer 2014), and most recently the Chinese BRIGHT-4 trial in STEMI primary PCI (Li 2022, Lancet). Reviews of the mechanism and early development include Gladwell (Clinical Therapeutics 2002), Warkentin and colleagues (Expert Opinion on Pharmacotherapy 2005), Deeks (Drugs 2008), and Lee and colleagues (British Journal of Clinical Pharmacology 2011).

What it does

In simple terms, bivalirudin stops blood from clotting for as long as it is being infused, then wears off quickly when the infusion is stopped. It does this by directly blocking thrombin — both thrombin that is free in the plasma and thrombin already trapped inside a clot — a property that heparin does not share, since heparin requires the cofactor antithrombin and cannot reach clot-bound thrombin effectively (Gladwell 2002; Lee 2011). The half-life is short (approximately 25 minutes in patients with normal kidney function), which is what gives bivalirudin its distinctive bleeding profile in PCI: anticoagulation can be turned off relatively quickly after the procedure ends. Compared with heparin (alone or with a glycoprotein IIb/IIIa inhibitor), bivalirudin has consistently produced less major bleeding in PCI populations across large randomized trials (Stone 2006; Stone 2008; Stone 2015; Li 2022).

Mechanism

Bivalirudin is a bivalent direct thrombin inhibitor: it bridges two separate sites on thrombin simultaneously. The N-terminal segment D-Phe-Pro-Arg-Pro docks into the catalytic active site (the Arg residue occupies the S1 specificity pocket where thrombin normally cleaves fibrinogen), and the C-terminal twelve residues (NGDFEEIPEEYL — derived from the C-terminus of natural hirudin) bind to exosite 1, the fibrinogen-recognition surface on thrombin. The two ends are connected by a flexible four-glycine linker. This bivalent architecture is what gives the molecule its high affinity and high specificity for thrombin (Gladwell 2002; Lee 2011). A distinguishing feature versus hirudin itself is that once bound, thrombin slowly cleaves the Arg-Pro scissile bond at the N-terminus of bivalirudin, partially restoring thrombin's enzymatic activity — this is one reason the drug's effect is reversible and wears off quickly compared with the essentially irreversible hirudins (Gladwell 2002; Lee 2011). Inhibition extends to both free and clot-bound thrombin. Elimination is partly renal (clearance is reduced in patients with renal impairment, and the half-life lengthens accordingly), with the remainder cleared by endogenous proteolysis (Gladwell 2002; Deeks 2008).

Evidence

  • Human: Extensive — multiple multi-thousand-patient randomized trials in PCI and acute coronary syndromes, summarized below.
  • Animal / in vitro: The bivalent binding mechanism and the slow active-site cleavage that defines bivalirudin's reversible profile have been characterized by enzymology and reviewed in the direct-thrombin-inhibitor literature (Gladwell 2002; Lee 2011; Kong 2014).

Landmark randomized trials, in order:

  • REPLACE-2 (Lincoff et al., JAMA 2003) — bivalirudin with provisional GP IIb/IIIa inhibition versus heparin with planned GP IIb/IIIa inhibition in contemporary urgent or elective PCI. Bivalirudin was non-inferior on ischemic endpoints and reduced major bleeding.
  • ACUITY (Stone et al., NEJM 2006; Stone et al., Lancet 2007) — bivalirudin in moderate- and high-risk acute coronary syndromes. Similar ischemic outcomes and significantly less bleeding than heparin plus GP IIb/IIIa; further analyzed in subgroups including diabetes (Feit 2008), saphenous-vein-graft PCI (Kumar 2010), and timing of clopidogrel (Lincoff 2008).
  • HORIZONS-AMI (Stone et al., NEJM 2008) — bivalirudin monotherapy vs heparin plus GP IIb/IIIa in STEMI primary PCI. Reduced 30-day major bleeding and 30-day all-cause mortality, with an early signal of increased acute (within 24 h) stent thrombosis. Long-term outcomes followed (Stone 2015, JACC).
  • EUROMAX (Steg et al., American Heart Journal 2013; Zeymer et al., European Heart Journal 2014; van 't Hof et al., European Heart Journal: Acute Cardiovascular Care 2017; Fabris et al., JAMA Cardiology 2017) — ambulance-initiated bivalirudin for STEMI transferred for primary PCI. Reduced bleeding versus heparin ± GP IIb/IIIa, with a similar early stent-thrombosis signal.
  • BRIGHT-4 (Li et al., Lancet 2022) — randomized 6,016 Chinese STEMI patients undergoing primary PCI to bivalirudin (with a 2- to 4-hour post-PCI high-dose infusion) versus heparin monotherapy. 30-day all-cause mortality was 2.96% with bivalirudin vs 3.92% with heparin (HR 0.75, 95% CI 0.57–0.99), and major (BARC 3-5) bleeding was 0.17% vs 0.80%, without an increase in reinfarction or stent thrombosis. Pre-specified subanalyses extended the result across bail-out GPI use (Liao 2024, BMC Medicine) and BMI strata (Zhang 2025, BMC Medicine); a ticagrelor-vs-clopidogrel analysis was reported in 2026 (Li 2026, Cardiovascular Revascularization Medicine); commentary appeared in JACC (Bivalirudin vs Heparin Anticoagulation in STEMI, 2024) and The Lancet (Piriou 2023; Li 2023 — Authors' reply). An updated meta-analysis incorporating BRIGHT-4 supports both mortality and bleeding benefit in STEMI (Oli 2023).

Across this body of work, the consistent finding is that bivalirudin reduces major bleeding versus heparin-plus-GP-IIb/IIIa regimens. The mortality picture has shifted over time as comparators (heparin monotherapy, post-procedure infusion strategies, radial access) have evolved, with BRIGHT-4 providing the most recent positive mortality signal in STEMI.

Known effects

  • Anticoagulation during PCI — FDA-approved indication (Deeks 2008); efficacy established across elective, urgent, and primary PCI (Lincoff 2003; Stone 2008; Li 2022).
  • Anticoagulation in patients with or at risk of HIT/HITTS — FDA-approved indication (Deeks 2008; Warkentin 2005; Lee 2011).
  • Reduced major bleeding vs heparin + GP IIb/IIIa in PCI — Phase III evidence across REPLACE-2, ACUITY, HORIZONS-AMI, and EUROMAX (Lincoff 2003; Stone 2006; Stone 2008; Zeymer 2014).
  • 30-day mortality reduction in STEMI primary PCI vs heparin monotherapy — most recently demonstrated in BRIGHT-4 (Li 2022) and supported by updated meta-analysis (Oli 2023).
  • Studied subgroups: acute coronary syndromes generally (Hartmann 2008; Singh 2007), patients with diabetes and ACS (Feit 2008), saphenous-vein-graft PCI (Kumar 2010), female AMI patients undergoing primary angioplasty (Liang 2016 — BRIGHT subgroup), elderly versus younger STEMI patients (Qaderdan 2017), and BMI strata (Zhang 2025).

Safety signals

The defining trade-off across the trial program has been between bleeding (consistently lower with bivalirudin versus heparin-based comparators) and acute (within 24 h) stent thrombosis (a small early excess seen with bivalirudin monotherapy in STEMI in HORIZONS-AMI and EUROMAX; not observed in BRIGHT-4 when a post-PCI high-dose infusion was added). The HORIZONS-AMI early stent-thrombosis signal was reported by Stone et al. (NEJM 2008) and revisited in longer follow-up (Stone 2015, JACC); the EUROMAX outcomes are reported by Steg et al. (American Heart Journal 2013) and Zeymer et al. (European Heart Journal 2014). In BRIGHT-4, the addition of a 2- to 4-hour post-PCI high-dose bivalirudin infusion eliminated the early stent-thrombosis excess while preserving the bleeding advantage (Li 2022). Pharmacokinetics are dose-linear with predictable prolongation in renal impairment (Gladwell 2002; Deeks 2008).

Regulatory status

  • US: Prescription-only injectable. FDA-approved as Angiomax (bivalirudin for injection) since December 2000; original indication was anticoagulation in patients with unstable angina undergoing PTCA, subsequently expanded to PCI including patients with or at risk of HIT/HITTS and to PCI with provisional GP IIb/IIIa inhibitor use (Deeks 2008).
  • EU: Marketed as Angiox; approved for use in adult patients undergoing PCI, including primary PCI for STEMI and acute coronary syndromes managed with urgent or early intervention (Deeks 2008; Steg 2013).
  • Class: Direct thrombin inhibitor (DTI) — same mechanistic class as hirudin, lepirudin, desirudin, and the small-molecule argatroban (Warkentin 2005; Lee 2011; Kong 2014).

Related peptides

  • Hirudin and its recombinant forms (lepirudin, desirudin) — the natural leech-derived direct thrombin inhibitors from which bivalirudin's C-terminal exosite-1-binding tail was derived (Gladwell 2002; Lee 2011).
  • Other agents in the same direct-thrombin-inhibitor class are discussed in the reviews by Warkentin (2005), Lee (2011), and Kong (2014).
Hypotheses6 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Could the blood-thinner bivalirudin accidentally turn back into a clot-promoter for a short window after a stent procedure?

If this holds, it would explain a puzzling pattern of blood clots seen in clinical trials and suggest that simply continuing the drug a few extra hours after the procedure (already tested in one trial) could prevent them. For the roughly one million patients who get stents each year, that is a potentially straightforward fix to a serious complication.

The hypothesis
The acute stent thrombosis signal observed with bivalirudin monotherapy in HORIZONS-AMI and EUROMAX is caused by rebound thrombin activity after the Arg-Pro scissile bond is cleaved, generating a thrombin molecule with partially restored catalytic activity that localizes to the stent surface before systemic bivalirudin clearance is complete, rather than by inadequate anticoagulant depth during the infusion.
Why it’s plausible
The readme establishes that thrombin slowly cleaves bivalirudin's Arg-Pro bond, partially restoring thrombin enzymatic function. If this cleavage rate is sufficiently fast relative to the half-life of bivalirudin itself (~25 min IV), a window exists during infusion where cleaved thrombin accumulates at the site of vessel injury (where thrombin generation is highest) before the drug is cleared. In BRIGHT-4, the stent thrombosis signal was abolished by extending the post-PCI bivalirudin infusion at high dose for 2-4 hours, which is consistent with suppressing rebound thrombin from accumulating on the stent surface rather than with simply maintaining anticoagulant depth, as a low-dose continued infusion would suffice for the latter.
Why it matters
If confirmed, this would establish that the rate of active-site cleavage is clinically relevant and should be a design parameter for next-generation direct thrombin inhibitors, favoring analogs with a slower or absent scissile-bond cleavage rate for PCI use while retaining the cleavage-mediated reversibility for non-stenting indications.
Plausibility.61
Novelty.63
Impact.69
Basis · grounding1 paper · 1 computed/note
[1]
paper
Thrombin cleaves the Arg-Pro scissile bond of bivalirudin, partially restoring thrombin activity; this is the mechanistic basis for reversibility.
doi: 10.1016/s0149-2918(02)85004-4
[2]
noteBRIGHT-4 protocol used a 2-4 hour post-PCI high-dose infusion and abolished the stent-thrombosis signal seen in HORIZONS-AMI with standard monotherapy cessation at end of procedure.
openupdated 2026-06-05

If you swap out the floppy bridge in the middle of bivalirudin for a more rigid one, could the drug work at a much lower dose?

If this works out, a next-generation version of bivalirudin might achieve the same anticoagulation with a fraction of the current dose, which could translate to less bleeding for patients undergoing heart procedures. Lower-dose anticoagulants with the same clot-preventing power have been a long-standing goal in cardiology.

The hypothesis
Replacing the flexible GGGG linker in bivalirudin with a conformationally constrained linker (e.g., a short Pro-Gly-Pro or beta-turn mimic) reduces the entropic cost of simultaneous bivalent binding to thrombin and increases apparent affinity by at least one order of magnitude without altering the scissile-bond cleavage rate.
Why it’s plausible
The four-glycine linker confers maximal flexibility but also imposes a large conformational entropy penalty when both termini are co-docked on thrombin. Structural studies of thrombin place the active site and exosite 1 at a fixed spatial separation; a semi-rigid linker of matching geometry would pre-organize the peptide for bivalent engagement, analogous to improvements seen in bivalent kinase inhibitors where rigid linkers dramatically increase potency. The cleavage rate at the Arg-Pro scissile bond is determined by the N-terminal FPRP geometry, not by the linker, so a linker substitution would decouple potency from reversibility.
Why it matters
A higher-affinity bivalirudin analog with the same reversibility and safety profile could achieve therapeutic anticoagulation at lower doses, reducing bleeding risk. This is directly relevant to the observed dose-dependent bleeding risk in PCI and would offer a next-generation direct thrombin inhibitor for the same indications.
Plausibility.73
Novelty.50
Impact.62
Basis · grounding1 paper · 1 computed/note
[1]
paper
The four-glycine linker connects the active-site and exosite-1 binding segments; the bivalent architecture is credited with high affinity and specificity for thrombin.
doi: 10.1016/s0149-2918(02)85004-4
[2]
sequenceSequence is FPRP-GGGG-NGDFEEIPEEYL; the four-glycine stretch is the sole structural determinant separating the two pharmacophore segments.
openupdated 2026-06-05

Could patients with a dangerous drug-induced clotting disorder (HIT) and failing kidneys be safely treated with bivalirudin injected under the skin at home, rather than by IV in a hospital?

HIT combined with severe kidney disease is a narrow but life-threatening situation with very few treatment options, especially outside large medical centers. If adjusted dosing of subcutaneous bivalirudin proved safe and effective here, it could give doctors a practical option for a patient group that currently has almost nowhere to turn.

The hypothesis
Subcutaneous bivalirudin, dosed to maintain trough plasma concentrations above the threshold needed to inhibit clot-bound thrombin, is clinically effective for extended outpatient anticoagulation in patients with acute HIT who cannot receive warfarin or novel oral anticoagulants due to concurrent severe renal impairment, without dose-accumulation toxicity if the infusion schedule accounts for the prolonged half-life under renal impairment.
Why it’s plausible
Axis-hit evidence confirms that subcutaneous bivalirudin produces detectable plasma levels for up to 6 hours with peak effect at 1-2h, and the readme notes that renal clearance is reduced in renal impairment, extending the half-life. HIT combined with severe renal impairment is a clinical scenario where argatroban (hepatic clearance, preferred in renal failure) is the guideline recommendation, but argatroban is not available in all countries. Bivalirudin's subcutaneous bioavailability opens the possibility of an outpatient regimen if the dose is adjusted for creatinine clearance, an approach that remains unstudied in prospective trials.
Why it matters
HIT in patients with stage 4-5 CKD is a narrow but high-mortality scenario with very limited options. Demonstrating that subcutaneous bivalirudin with renal-adjusted dosing achieves therapeutic anticoagulation in this population would fill a genuine therapeutic gap and leverage an existing approved drug without new synthesis.
Plausibility.50
Novelty.53
Impact.52
Basis · grounding2 papers
[1]
paper
Subcutaneous bivalirudin produces sustained anticoagulant effects for a few hours; peak at 1-2h, detectable levels up to 6h post-injection; half-life extends in renal impairment.
doi: 10.1517/14656566.6.8.1349
[2]
paper
Bivalirudin is FDA-approved for HIT; renal clearance is a component of elimination and clearance is reduced in renal impairment.
doi: 10.1517/14656566.6.8.1349
openupdated 2026-06-05

Does bivalirudin accidentally preserve the body's built-in system for limiting clots, explaining why it causes less bleeding than older blood thinners?

If confirmed, this would reveal a previously unknown reason why bivalirudin causes less bleeding than heparin, and could guide the design of even safer anticoagulants. For patients who need strong blood thinners but are also at high bleeding risk, such as elderly patients or those on multiple medications, a drug that selectively spares this protective pathway could be genuinely safer.

The hypothesis
Bivalirudin's exosite-1 C-terminal segment (NGDFEEIPEEYL) binds thrombomodulin-bound thrombin with lower affinity than free thrombin, because thrombomodulin occupancy of exosite 1 sterically displaces the bivalirudin tail, causing selective sparing of the thrombomodulin-thrombin complex and preservation of protein C activation even during bivalirudin infusion.
Why it’s plausible
Thrombomodulin binds thrombin exosite 1 to redirect thrombin toward protein C activation, an endogenous anticoagulant pathway. Since bivalirudin's C-terminal tail also binds exosite 1, the two ligands compete. If thrombomodulin wins this competition (due to higher affinity or larger buried surface), bivalirudin would selectively inhibit fibrinogen-cleaving free thrombin while leaving the pro-anticoagulant thrombomodulin-thrombin complex active. This selectivity could partly explain bivalirudin's superior bleeding profile versus heparin, which does not preserve protein C activation selectively.
Why it matters
Demonstrating that bivalirudin selectively spares thrombomodulin-bound thrombin would identify a previously unrecognized mechanism of bleeding-sparing efficacy and would motivate engineering new thrombin inhibitors that are even more selective for free versus thrombomodulin-bound thrombin as a strategy to reduce bleeding without reducing anticoagulant efficacy.
Plausibility.43
Novelty.59
Impact.58
Basis · grounding2 papers
[1]
paper
Bivalirudin C-terminal tail derived from hirudin binds thrombin exosite 1, the same surface used by thrombomodulin; competitive displacement is not discussed.
doi: 10.1016/s0149-2918(02)85004-4
[2]
paper
Mechanisms through which bivalirudin provides bleeding benefit beyond simple thrombin blockade deserve further study.
doi: 10.1016/j.jacc.2014.10.029
openupdated 2026-06-05

In a life-threatening infection where the blood and immune system spiral out of control together, could bivalirudin do double duty by reducing both clotting and inflammation?

Sepsis kills roughly 11 million people a year worldwide, and the clotting and inflammation feed each other in a vicious cycle. If bivalirudin could interrupt that cycle through two separate mechanisms, it might offer a meaningful advantage over current options. This is still an early idea, but the underlying biology and the drug's safety record make it worth investigating.

The hypothesis
Bivalirudin can attenuate thrombin-driven PAR1 and PAR4 signaling on endothelial cells and macrophages in sepsis-associated coagulopathy, reducing inflammatory cytokine release independently of its anticoagulant effect on fibrin formation.
Why it’s plausible
Thrombin activates protease-activated receptors PAR1 and PAR4, driving NF-kB-mediated inflammation. Bivalirudin's N-terminal FPRP segment occupies the thrombin active site and blocks substrate cleavage of PARs, while exosite-1 occupancy by the C-terminal tail may additionally interfere with PAR tethered-ligand docking. In sepsis, the thrombin-PAR axis amplifies organ damage beyond clot formation. Bivalirudin's low immunogenicity and reversible pharmacokinetics make it mechanistically suited to a short-course immunomodulatory use in sepsis-associated disseminated intravascular coagulation (DIC).
Why it matters
Sepsis-associated DIC has no approved direct thrombin inhibitor; current standard of care uses heparin which cannot access clot-bound thrombin and has high bleeding risk. Establishing a PAR-suppression mechanism for bivalirudin would provide a second rationale for its use in sepsis beyond anticoagulation and could widen its clinical scope to inflammatory conditions driven by thrombin signaling.
Plausibility.64
Novelty.27
Impact.53
Basis · grounding2 papers
[1]
paper
Bivalirudin blocks both free and clot-bound thrombin; heparin cannot reach clot-bound thrombin and requires antithrombin cofactor.
doi: 10.1016/s0149-2918(02)85004-4
[2]
paper
Authors note that the mechanisms through which bivalirudin provides its benefits deserve further study, suggesting incompletely understood anti-inflammatory or non-anticoagulant contributions.
doi: 10.1016/j.jacc.2014.10.029
openupdated 2026-06-05

Is one unusual ingredient in bivalirudin pulling double duty: both shielding the drug from being broken down and directly boosting how tightly it binds to its target?

If this is true, it would change a widespread assumption in drug design. Chemists routinely use mirror-image amino acids only as a protective trick, not expecting them to improve binding on their own. Showing that they can do both would give medicinal chemists a new design principle for building better peptide drugs against clotting and potentially many other targets.

The hypothesis
The D-phenylalanine at position 1 of bivalirudin, beyond protecting against aminopeptidase cleavage, contributes directly to affinity for the thrombin S1 prime pocket through a stereospecific hydrophobic contact that the L-isomer cannot make, such that replacing D-Phe with L-Phe reduces thrombin inhibitory potency by more than 10-fold.
Why it’s plausible
The readme states the N-terminal D-Phe protects the active-site contact from rapid proteolysis, implying its primary role is metabolic stability. However, D-amino acids at P positions of thrombin substrates and inhibitors can adopt backbone dihedral angles inaccessible to L-amino acids, potentially positioning the phenyl ring into a hydrophobic sub-pocket adjacent to S1 in a way that the L-isomer cannot. If the D-stereocentre provides a direct binding contribution, not merely proteolytic protection, this fundamentally changes the design rule for thrombin-targeting peptides.
Why it matters
Most peptide-engineering programs routinely substitute D-amino acids at termini for metabolic protection. Establishing that the D-Phe at position 1 of bivalirudin also drives affinity would be a clear demonstration that D-residues can carry dual roles (stability plus pharmacophore), shaping rules for medicinal chemistry of bivalent thrombin inhibitors.
Plausibility.67
Novelty.30
Impact.45
Basis · grounding1 paper · 1 computed/note
[1]
paper
D-phenylalanine at the N-terminus is explicitly described as protecting the active-site contact from rapid proteolysis, with its affinity contribution left unquantified.
doi: 10.1016/s0149-2918(02)85004-4
[2]
noteBivalirudin was designed as a synthetic mimic of hirudin; the D-Phe substitution at the N-terminus was a medicinal chemistry choice during the Hirulog program at Biogen.
details expand to inspect
3-letter notation
Phe-Pro-Arg-Pro-Gly-Gly-Gly-Gly-Asn-Gly-Asp-Phe-Glu-Glu-Ile-Pro-Glu-Glu-Tyr-Leu
citationbibtex
peptidemodel (2026). Bivalirudin: Angiomax/Angiox blood-clot preventer used during heart procedures (pep-04426, v1). PeptideModel. https://peptidemodel.com/card/pep-04426
@peptide{pep04426,
  sequence = {FPRPGGGGNGDFEEIPEEYL},
  target   = {},
  author   = {peptidemodel},
  year     = {2026},
  status   = {bioassayed}
}
clinical trials 105 on ct.gov · 25 on EUCTR · checked 2026-05-22
ct.gov trials 105
with results 15
EUCTR 25
PubMed RCT 225
by phase
3phase 35phase 42no phase
by status
5completed1recruiting2terminated1withdrawn1unknown
references 30 papers
[2] supporting
[3] supporting
[4]
Bivalirudin: a review
Warkentin, T. et al. Expert Opinion on Pharmacotherapy 2005
supporting
[5]
Bivalirudin for Patients with Acute Coronary Syndromes
Stone, G. et al. New England Journal of Medicine 2006
supporting
[9] supporting
[11] supporting
[14]
Direct thrombin inhibitors
Lee, C. et al. British Journal of Clinical Pharmacology 2011
supporting
[16] supporting
[24] supporting
[28]
Bivalirudin vs Heparin Anticoagulation in STEMI
Stone, G. et al. Journal of the American College of Cardiology 2024
supporting
discussion no comments
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