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Identification
- Generic Name
- Alfimeprase
- DrugBank Accession Number
- DB04919
- Background
Alfimeprase is a recombinant analog of fibrolase. Fibrolase is a zinc-containing metalloproteinase isolated from the venom of the southern copperhead snake (Agkistrodon contortrix contortrix). It is a small protein that contains 203 residues (Randolph et al. 1992). Alfimeprase is being developed by Nuvelo.
- Type
- Biotech
- Groups
- Investigational
- Biologic Classification
- Protein Based Therapies
Other protein based therapies - Protein Chemical Formula
- Not Available
- Protein Average Weight
- Not Available
- Sequences
>Alfimeprase Sequence SFPQRYVQLVIVADHRMNTKYNGDSDKIRQWVHQIVNTINEIYRPLNIQFTLVGLEIWSN QDLITVTSVSHDTLASFGNWRETDLLRRQRHDNAQLLTAIDFDGDTVGLAYVGGMCQLKH STGVIQDHSAINLLVALTMAHELGHNLGMNHDGNQCHCGANSCVMAAMLSDQPSKLFSDC SKKDYQTFLTVNNPQCILNKP
Download FASTA Format- Synonyms
- 3-203-FIBROLASE (3-SERINE) (AGKISTRODON CONTORTRIX CONTORTRIX RECOMBINANT)
- Alfimeprase
Pharmacology
- Indication
Alfimeprase is being evaluated as a potential treatment for acute ischemic stroke, catheter occlusion (CO) and acute peripheral arterial occlusion (PAO).
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Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
Alfimeprase is a recombinant direct acting fibrinolytic (rDAF), or blood clot dissolver, that has the potential to rapidly and directly degrade fibrin, a protein that provides the scaffolding for blood clots, when delivered through a catheter to the site of a blood clot.
- Mechanism of action
When delivered locally at the site of a blood clot, alfimeprase has the potential, through a unique mechanism of action, to directly and rapidly degrade fibrin, a protein that provides the scaffolding for blood clots. In addition, alfimeprase's thrombolytic activity appears to be localized to the site of delivery because it is rapidly inactivated by alpha-2 macroglobulin, a naturally occurring protein in the blood, as it moves away from the site of delivery and into the general blood circulation.
Target Actions Organism UFibrinogen alpha chain Not Available Humans UFibrinogen beta chain Not Available Humans - Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Not Available
- Pathways
- Not Available
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- Not Available
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- Not Available
- Kingdom
- Organic Compounds
- Super Class
- Organic Acids
- Class
- Carboxylic Acids and Derivatives
- Sub Class
- Amino Acids, Peptides, and Analogues
- Direct Parent
- Peptides
- Alternative Parents
- Not Available
- Substituents
- Not Available
- Molecular Framework
- Not Available
- External Descriptors
- Not Available
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- GPN9HBH1HS
- CAS number
- 259074-76-5
References
- General References
- Jones G, Ronk M, Mori F, Zhang Z: Disulfide structure of alfimeprase: a recombinant analog of fibrolase. Protein Sci. 2001 Jun;10(6):1264-7. [Article]
- External Links
- PubChem Substance
- 347909847
Clinical Trials
- Clinical Trials
Clinical Trial & Rare Diseases Add-on Data Package
Explore 4,000+ rare diseases, orphan drugs & condition pairs, clinical trial why stopped data, & more. Preview package Phase Status Purpose Conditions Count Start Date Why Stopped 100+ additional columns Unlock 175K+ rows when you subscribe.View sample data3 Completed Treatment Arterial Occlusive Diseases 1 somestatus stop reason just information to hide 3 Completed Treatment Catheter Occlusion / Thrombosis / Venous Thrombosis (Disorder) 1 somestatus stop reason just information to hide 3 Completed Treatment Thrombosis / Venous Thrombosis (Disorder) 1 somestatus stop reason just information to hide 3 Terminated Treatment Arterial Occlusive Diseases 1 somestatus stop reason just information to hide 2 Completed Treatment Arterial Occlusive Diseases / Peripheral Vascular Disease Patient / Thrombosis 1 somestatus stop reason just information to hide
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Liquid
- Experimental Properties
- Not Available
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways
- Specific Function
- extracellular matrix structural constituent
- Gene Name
- FGA
- Uniprot ID
- P02671
- Uniprot Name
- Fibrinogen alpha chain
- Molecular Weight
- 94972.455 Da
References
- Ahmed NK, Tennant KD, Markland FS, Lacz JP: Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom. Haemostasis. 1990;20(3):147-54. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways
- Specific Function
- extracellular matrix structural constituent
- Gene Name
- FGB
- Uniprot ID
- P02675
- Uniprot Name
- Fibrinogen beta chain
- Molecular Weight
- 55927.9 Da
References
- Ahmed NK, Tennant KD, Markland FS, Lacz JP: Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom. Haemostasis. 1990;20(3):147-54. [Article]
Drug created at October 21, 2007 22:23 / Updated at September 30, 2023 19:51