Detailed description page of THPdb

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Th1036 details

Primary information
ID 1257
ThPP ID Th1036
Therapeutic Peptide/Protein Name Aldesleukin
Sequence MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification Ib
Molecular Weight 15314.8
Chemical Formula C690H1115N177O202S6
Isoelectric Point 7.31
Hydrophobicity -0.192
Melting Point (℃) N.A.
Half Life 0.22-1.42 hours
Description Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution 0.18 l/kg
Clearance The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories Antineoplastic Agents
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Corticosteroids such as clobetasol propionate may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
Target Interleukin-2 receptor subunit beta,Interleukin-2 receptor subunit alpha,Cytokine receptor common subunit gamma
Information of corresponding available drug in the market
Brand Name Proleukin
Company Chiron Corp
Brand Discription Proleukin, a human recombinant interleukin-2 product, is a highly purified protein with a molecular weight of approximately 15,300 daltons. It is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of
Prescribed for Treating skin cancer and kidney cancer that has spread to other parts of the body.
Chemical Name desalanyl-1, serine-125 human interleukin-2
Formulation Proleukin is supplied in single-use vials intended for intravenous administration. When reconstituted with 1.2 mL Sterile Water for Injection, USP, each mL contains 18 million International Units (1.1 mg) Proleukin, 50 mg mannitol, and 0.18 mg sodium dod
Physcial Appearance Sterile, white to off-white, lyophilized cake
Route of Administration Intravenous administration
Recommended Dosage The recommended Proleukin treatment regimen is administered by a 15 minute Intravenous infusion every 8 hours. 600,000 International Units/kg (0.037 mg/kg) dose administered every 8 hours by a 15 minute Intravenous infusion for a maximum of 14 doses. ollowing 9 days of rest, the schedule is repeated for another 14 doses, for a maximum of 28 doses per course, as tolerated.
Contraindication Proleukin is contraindicated in patients with a known history of hypersensitivity to interleukin-2 or any component of the Proleukin formulation.
Side Effects Anxiety; dizziness; general body discomfort; increased cough; infection; loss of appetite; pain; runny nose; weakness.
Useful Link http://www.rxlist.com/proleukin-drug.htm
PubMed ID 25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure Th1036 (View) or (Download)

Primary information
ID 1258
ThPP ID Th1036
Therapeutic Peptide/Protein Name Aldesleukin
Sequence MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification Ib
Molecular Weight 15314.8
Chemical Formula C690H1115N177O202S6
Isoelectric Point 7.31
Hydrophobicity -0.192
Melting Point (℃) N.A.
Half Life 0.22-1.42 hours
Description Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution 0.18 l/kg
Clearance The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories Anti-HIV Agents
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Corticosteroids such as clocortolone may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
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 Proleukin is contraindicated in patients with an abnormal thallium stress test or abnormal pulmonary function tests and those with organ allografts. Retreatment with Proleukin is contraindicated in patients who have experienced the following drug-related
Side Effects Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; black stools; chest pain; chills; confusion; depression; diarrhea; drowsiness; fainting; fever; heart murmurs or gallops; infrequent urination.
Useful Link http://www.drugs.com/cdi/proleukin.html
PubMed ID 25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure Th1036 (View) or (Download)

Primary information
ID 1259
ThPP ID Th1036
Therapeutic Peptide/Protein Name Aldesleukin
Sequence MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification Ib
Molecular Weight 15314.8
Chemical Formula C690H1115N177O202S6
Isoelectric Point 7.31
Hydrophobicity -0.192
Melting Point (℃) N.A.
Half Life 0.22-1.42 hours
Description Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity N.A.
Metabolism N.A.
Absorption N.A.
Volume of Distribution 0.18 l/kg
Clearance The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories N.A.
Patents Number N.A.
Date of Issue N.A.
Date of Expiry N.A.
Drug Interaction Corticosteroids such as corticotropin may diminish the antineoplastic effect of Aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
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 N.A.
Side Effects N.A.
Useful Link http://www.drugs.com/drug-interactions/aldesleukin,proleukin-index.html
PubMed ID 25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure Th1036 (View) or (Download)

OSDDlinux

Raghava's Group

IMTECH

CSIR

CRDD
CPPSITE 2.0

Primary information
ID	1257
ThPP ID	Th1036
Therapeutic Peptide/Protein Name	Aldesleukin
Sequence	MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification	Ib
Molecular Weight	15314.8
Chemical Formula	C690H1115N177O202S6
Isoelectric Point	7.31
Hydrophobicity	-0.192
Melting Point (℃)	N.A.
Half Life	0.22-1.42 hours
Description	Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease	For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics	Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action	Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	0.18 l/kg
Clearance	The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories	Antineoplastic Agents
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Corticosteroids such as clobetasol propionate may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
Target	Interleukin-2 receptor subunit beta,Interleukin-2 receptor subunit alpha,Cytokine receptor common subunit gamma
Information of corresponding available drug in the market
Brand Name	Proleukin
Company	Chiron Corp
Brand Discription	Proleukin, a human recombinant interleukin-2 product, is a highly purified protein with a molecular weight of approximately 15,300 daltons. It is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of
Prescribed for	Treating skin cancer and kidney cancer that has spread to other parts of the body.
Chemical Name	desalanyl-1, serine-125 human interleukin-2
Formulation	Proleukin is supplied in single-use vials intended for intravenous administration. When reconstituted with 1.2 mL Sterile Water for Injection, USP, each mL contains 18 million International Units (1.1 mg) Proleukin, 50 mg mannitol, and 0.18 mg sodium dod
Physcial Appearance	Sterile, white to off-white, lyophilized cake
Route of Administration	Intravenous administration
Recommended Dosage	The recommended Proleukin treatment regimen is administered by a 15 minute Intravenous infusion every 8 hours. 600,000 International Units/kg (0.037 mg/kg) dose administered every 8 hours by a 15 minute Intravenous infusion for a maximum of 14 doses. ollowing 9 days of rest, the schedule is repeated for another 14 doses, for a maximum of 28 doses per course, as tolerated.
Contraindication	Proleukin is contraindicated in patients with a known history of hypersensitivity to interleukin-2 or any component of the Proleukin formulation.
Side Effects	Anxiety; dizziness; general body discomfort; increased cough; infection; loss of appetite; pain; runny nose; weakness.
Useful Link	http://www.rxlist.com/proleukin-drug.htm
PubMed ID	25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure	Th1036 (View) or (Download)

Primary information
ID	1258
ThPP ID	Th1036
Therapeutic Peptide/Protein Name	Aldesleukin
Sequence	MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification	Ib
Molecular Weight	15314.8
Chemical Formula	C690H1115N177O202S6
Isoelectric Point	7.31
Hydrophobicity	-0.192
Melting Point (℃)	N.A.
Half Life	0.22-1.42 hours
Description	Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease	For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics	Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action	Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	0.18 l/kg
Clearance	The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories	Anti-HIV Agents
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Corticosteroids such as clocortolone may diminish the antineoplastic effect of aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
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	Proleukin is contraindicated in patients with an abnormal thallium stress test or abnormal pulmonary function tests and those with organ allografts. Retreatment with Proleukin is contraindicated in patients who have experienced the following drug-related
Side Effects	Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; black stools; chest pain; chills; confusion; depression; diarrhea; drowsiness; fainting; fever; heart murmurs or gallops; infrequent urination.
Useful Link	http://www.drugs.com/cdi/proleukin.html
PubMed ID	25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure	Th1036 (View) or (Download)

Primary information
ID	1259
ThPP ID	Th1036
Therapeutic Peptide/Protein Name	Aldesleukin
Sequence	MAPTSSSTKKTQLQLEHLLLDLQMILNGINNYKNPKLTRMLTFKFYMPKK view full sequnce in fasta
Functional Classification	Ib
Molecular Weight	15314.8
Chemical Formula	C690H1115N177O202S6
Isoelectric Point	7.31
Hydrophobicity	-0.192
Melting Point (℃)	N.A.
Half Life	0.22-1.42 hours
Description	Aldesleukin, a lymphokine, is produced by recombinant DNA technology using a genetically engineered E. coli strain containing an analog of the human interleukin-2 gene. Genetic engineering techniques were used to modify the human IL-2 gene, and the resulting expression clone encodes a modified human interleukin-2. This recombinant form differs from native interleukin-2 in the following ways: a) Aldesleukin is not glycosylated because it is derived from E. coli; b) the molecule has no N-terminal alanine; the codon for this amino acid was deleted during the genetic engineering procedure; c) the molecule has serine substituted for cysteine at amino acid position 125.
Indication/Disease	For treatment of adults with metastatic renal cell carcinoma.
Pharmacodynamics	Aldesleukin is used to treat renal cell carcinoma, it induces the enhancement of lymphocyte mitogenesis and stimulation of long-term growth of human interleukin-2 dependent cell lines, the enhancement of lymphocyte cytotoxicity, the induction of killer cell (lymphokine-activated (LAK) and natural (NK)) activity; and the induction of interferon-gamma production. IL-2 is normally produced by the body, secreted by T cells, and stimulates growth and differentiation of T cell response. It can be used in immunotherapy to treat cancer. It enhances the ability of the immune system to kill tumor cells and may interfere with blood flow to the tumor.
Mechanism of Action	Aldesleukin binds to the IL-2 receptor which leads to heterodimerization of the cytoplasmic domains of the IL-2R beta and gamma chains, activation of the tyrosine kinase Jak3, and phosphorylation of tyrosine residues on the IL-2R beta chain. These events led to the creation of an activated receptor complex, to which various cytoplasmic signaling molecules are recruited and become substrates for regulatory enzymes (especially tyrosine kinases) that are associated with the receptor. These events stimulate growth and differentiation of T cells.
Toxicity	N.A.
Metabolism	N.A.
Absorption	N.A.
Volume of Distribution	0.18 l/kg
Clearance	The pharmacokinetic profile of Proleukin is characterized by high plasma concentrations following a short IV infusion, rapid distribution into the extravascular space and elimination from the body by metabolism in the kidneys with little or no bioactive p
Categories	N.A.
Patents Number	N.A.
Date of Issue	N.A.
Date of Expiry	N.A.
Drug Interaction	Corticosteroids such as corticotropin may diminish the antineoplastic effect of Aldesleukin. Avoid conccurent use of corticosteroids with aldesleukin.
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	N.A.
Side Effects	N.A.
Useful Link	http://www.drugs.com/drug-interactions/aldesleukin,proleukin-index.html
PubMed ID	25589384, 25270293, 25270293, 24598453, 11980386, 25270293, 23386066, 11980386
3-D Structure	Th1036 (View) or (Download)

Updated version of this database is available at ThpDB2

Detailed description page of THPdb