Primary information |
---|
ID | 1055 |
ThPP ID | Th1009 |
Therapeutic Peptide/Protein Name | Alteplase |
Sequence | SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKS view full sequnce in fasta |
Functional Classification | Ib |
Molecular Weight | 59042.3 |
Chemical Formula | C2569H3928N746O781S40 |
Isoelectric Point | 7.61 |
Hydrophobicity | -0.516 |
Melting Point (℃) | 60 |
Half Life | N.A. |
Description | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. |
Indication/Disease | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli |
Pharmacodynamics | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. |
Mechanism of Action | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | Thrombolytic Agents |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Ginkgo biloba.Additive anticoagulant/antiplatelet effects may increase bleeding risk. Concomitant therapy should be avoided. |
Target | Plasminogen,Fibrinogen alpha chain,Urokinase plasminogen activator surface receptor,Plasminogen activator inhibitor 1 |
Information of corresponding available drug in the market |
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Brand Name | Activase |
Company | Genentech Inc |
Brand Discription | Activase is a tissue plasminogen activator produced by recombinant DNA technology. It is a sterile, purified glycoprotein of 527 amino acids, synthesized using the complementary DNA (cDNA) for natural human tissue-type plasminogen activator obtained from |
Prescribed for | To treat blood clots in the lungs and improve heart function and survival followed by a heart attack. Activase may also be used to improve recovery and reduce disability in certain patients who have suffered from a stroke. |
Chemical Name | N.A. |
Formulation | N.A. |
Physcial Appearance | Sterile, white to off-white, lyophilized powder |
Route of Administration | Intravenous |
Recommended Dosage | The recommended dose is not to exceed 100 mg. Patients weighing > 67 kg are recommended a dose of 100 mg as a 15 mg intravenous bolus, followed by 50 mg infused over the next 30 minutes, and then 35 mg infused over the next 60 minutes. |
Contraindication | Allergic |
Side Effects | Rash; hives; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue. |
Useful Link | http://www.drugs.com/cdi/activase.html |
PubMed ID | 15650539 |
3-D Structure | Th1009 (View) or (Download) |
Primary information |
---|
ID | 1056 |
ThPP ID | Th1009 |
Therapeutic Peptide/Protein Name | Alteplase |
Sequence | SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKS view full sequnce in fasta |
Functional Classification | Ib |
Molecular Weight | 59042.3 |
Chemical Formula | C2569H3928N746O781S40 |
Isoelectric Point | 7.61 |
Hydrophobicity | -0.516 |
Melting Point (℃) | 60 |
Half Life | N.A. |
Description | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. |
Indication/Disease | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli |
Pharmacodynamics | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. |
Mechanism of Action | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | Thrombolytic Agents |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | IV nitroglycerin may decrease the effect of alteplase. |
Target | N.A. |
Information of corresponding available drug in the market |
---|
Brand Name | N.A. |
Company | N.A. |
Brand Discription | N.A. |
Prescribed for | N.A. |
Chemical Name | N.A. |
Formulation | N.A. |
Physcial Appearance | N.A. |
Route of Administration | N.A. |
Recommended Dosage | N.A. |
Contraindication | Have active internal bleeding, history of stroke, recent brain or spinal surgery (within 3 months), a growth in the brain, abnormal formation of blood vessels. |
Side Effects | Black or bloody stools; bloody vomit; change in color of your fingers or toes; changes in vision; chills; coughing up blood; decreased amount of urine produced; difficulty breathing or sudden shortness of breath; difficulty swallowing. |
Useful Link | http://www.rxlist.com/activase-drug.htm |
PubMed ID | 15650539 |
3-D Structure | Th1009 (View) or (Download) |
Primary information |
---|
ID | 1057 |
ThPP ID | Th1009 |
Therapeutic Peptide/Protein Name | Alteplase |
Sequence | SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKS view full sequnce in fasta |
Functional Classification | Ib |
Molecular Weight | 59042.3 |
Chemical Formula | C2569H3928N746O781S40 |
Isoelectric Point | 7.61 |
Hydrophobicity | -0.516 |
Melting Point (℃) | 60 |
Half Life | N.A. |
Description | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. |
Indication/Disease | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli |
Pharmacodynamics | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. |
Mechanism of Action | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | Thrombolytic Agents |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Ticlopidine.Increased bleeding risk. Monitor for signs of bleeding. |
Target | N.A. |
Information of corresponding available drug in the market |
---|
Brand Name | N.A. |
Company | N.A. |
Brand Discription | N.A. |
Prescribed for | N.A. |
Chemical Name | N.A. |
Formulation | N.A. |
Physcial Appearance | N.A. |
Route of Administration | N.A. |
Recommended Dosage | N.A. |
Contraindication | Certain type of bulging blood vessel (aneurysm), have a heart attack or blood clot in the lung and you also have had recent brain or spinal injury |
Side Effects | Numbness in arm or leg; one-sided weakness; pain, redness, or swelling at the injection site; purple skin color; rectal bleeding; seizures; severe bleeding; severe muscle aches or pain; severe stomach pain; sharp or crushing chest pain; speech problems |
Useful Link | http://www.drugs.com/drug-interactions/alteplase,activase-index.html?filter=1 |
PubMed ID | 15650539 |
3-D Structure | Th1009 (View) or (Download) |
Primary information |
---|
ID | 1058 |
ThPP ID | Th1009 |
Therapeutic Peptide/Protein Name | Alteplase |
Sequence | SYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKS view full sequnce in fasta |
Functional Classification | Ib |
Molecular Weight | 59042.3 |
Chemical Formula | C2569H3928N746O781S40 |
Isoelectric Point | 7.61 |
Hydrophobicity | -0.516 |
Melting Point (℃) | 60 |
Half Life | N.A. |
Description | Glycosylated, human tissue plasminogen activator of 527 residues purified from CHO cells. |
Indication/Disease | To manage acute myocardial infarction, acute ischemic stroke and for lysis of acute pulmonary emboli |
Pharmacodynamics | Alteplase binds to fibrin in a thrombus and converts the entrapped plasminogen to plasmin, thus limited conversion of plasminogen takes place in the absence of fibrin. |
Mechanism of Action | Alteplase on binding to fibrin rich clots via the fibronectin finger-like domain and the Kringle 2 domain cleaves (domain) the Arg/Val bond in plasminogen to form plasmin which in turn degrades the fibrin matrix of the thrombus, thereby exerting its thrombolytic action. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | Thrombolytic Agents |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | N.A. |
Target | N.A. |
Information of corresponding available drug in the market |
---|
Brand Name | N.A. |
Company | N.A. |
Brand Discription | N.A. |
Prescribed for | N.A. |
Chemical Name | N.A. |
Formulation | N.A. |
Physcial Appearance | N.A. |
Route of Administration | N.A. |
Recommended Dosage | N.A. |
Contraindication | History of bleeding problems, or severe uncontrolled high blood pressure. |
Side Effects | Sudden arm or leg pain; sudden dizziness, fainting, severe headache, or vomiting; unusual or easy bleeding or bruising. |
Useful Link | N.A. |
PubMed ID | 15650539 |
3-D Structure | Th1009 (View) or (Download) |