Identification
- Summary
Recombinant alpha 1-antitrypsin is a medication indicated to treat patients with chronic alpha1-proteinase inhibitor deficiency.
- Generic Name
- Recombinant alpha 1-antitrypsin
- DrugBank Accession Number
- DB05481
- Background
Alpha 1-antitrypsin is a glycoprotein primarily produced by hepatocytes, and to a lesser extent, immune system cells. Recombinant alpha 1-antitrypsin (rAAT) is produced from yeast, which unlike commercially available forms of plasma-derived AAT, eliminates the risk associated with blood-borne infectious agents and allows for a increased manufacturing. rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase. The proteinase/antiproteinase balance is believed to be important for maintaining healthy skin. The rAAT topical gel (Dermolastin™) is indicated for patients with atopic dermatitis and psoriasis. The company has indicated that other formulations for gastroenterological and urological indications will also be developed.
- Type
- Biotech
- Groups
- Investigational
- Biologic Classification
- Protein Based Therapies
Other protein based therapies - Protein Chemical Formula
- Not Available
- Protein Average Weight
- Not Available
- Sequences
- Not Available
- Synonyms
- Recombinant alpha 1-antitrypsin
Pharmacology
- Indication
Investigated for use/treatment in alpha 1 antitrypsin deficiency, atopic dermatitis, and chronic obstructive pulmonary disease (COPD).
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Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Management of Alpha 1-antitrypsin deficiency •••••••••••• •••••••••• ••••••••• ••••••• ••• •••••••• - Contraindications & Blackbox Warnings
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Alpha 1-antitrypsin is a glycoprotein primarily produced by hepatocytes, and to a lesser extent, immune system cells. Recombinant alpha 1-antitrypsin (rAAT) is produced from yeast, which unlike commercially available forms of plasma-derived AAT, eliminates the risk associated with blood-borne infectious agents and allows for a increased manufacturing. rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase. The proteinase/antiproteinase balance is believed to be important for maintaining healthy skin.
- Mechanism of action
rAAT belongs to a family of structurally-related proteins classified as serine protease inhibitors or SERPINS, which are known to inhibit several proteases including trypsin, cathepsin G, thrombin, tissue kallikrein, as well as neutrophil elastase.
Target Actions Organism UAlpha-1-antitrypsin 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
Well tolerated in clinical trials.
- 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
Products
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- Dermolastin
Categories
- Drug Categories
- Not Available
- 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
- Not Available
Chemical Identifiers
- UNII
- Not Available
- CAS number
- Not Available
References
- General References
- External Links
- PubChem Substance
- 347910164
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Withdrawn Treatment Alpha-1 Anti-trypsin Deficiency / Chronic Obstructive Pulmonary Disease (COPD) 1 1, 2 Completed Treatment Alpha-1 Anti-trypsin Deficiency 2
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Powder, for solution Intravenous 1000 MG/40ML Powder, for solution Parenteral 1000 MG/40ML Powder, for solution Parenteral 4000 MG Powder, for solution Parenteral 5000 MG Powder, for solution Powder, for solution Intravenous; Parenteral 4000 MG Powder, for solution Intravenous; Parenteral 5000 MG Powder, for solution 1000 MG Powder, for solution 500 MG Solution, concentrate Intravenous 1 g - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
- Not Available
Targets
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Serine-type endopeptidase inhibitor activity
- Specific Function
- Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. T...
- Gene Name
- SERPINA1
- Uniprot ID
- P01009
- Uniprot Name
- Alpha-1-antitrypsin
- Molecular Weight
- 46736.195 Da
Drug created at November 18, 2007 18:25 / Updated at September 29, 2023 14:17