| Entry 1 |
| (1) Primary information |
|---|
| ID | 1205 |
| ThPP ID | Th1027 |
| Therapeutic Peptide/Protein Name | Insulin Regular |
| Sequence | A-chain:GIVEQCCTSICSLYQLENYCN B-chain:FVNQHLCGSHLV view full sequnce in fasta |
| Functional Classification | Ia |
| Molecular Weight | 5.808 |
| Chemical Formula | C257H383N65O77S6 |
| Isoelectric Point | 5.39 |
| Hydrophobicity | 0.218 |
| Melting Point (℃) | 81 |
| Half Life | N.A. |
| Description | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. |
| Indication/Disease | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. |
| Pharmacodynamics | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. |
| Mechanism of Action | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. |
| Toxicity | Hypoglycemia is caused due to insulin toxicity. |
| Metabolism | Predominantly cleared by metabolic degradation via a receptor-mediated process. |
| Absorption | Generally well absorbed. |
| Volume of Distribution | 0.15 L/kg |
| Clearance | N.A. |
| Categories | Antidiabetic Agents |
| Patents Number | N.A. |
| Date of Issue | N.A. |
| Date of Expiry | N.A. |
| Drug Interaction | Liraglutide's coadministration may increase the risk of hypoglycemia. A lower dose of the antidiabetic agent may be needed. |
| Target | Insulin receptor,Insulin-like growth factor 1 receptor,Retinoblastoma-associated protein,Cathepsin D,Insulin-degrading enzyme,Neuroendocrine convertase 2,Carboxypeptidase E,Neuroendocrine convertase 1,Protein NOV homolog,Low-density lipoprotein receptor-r |
| Information of corresponding available drug in the market |
|---|
| Brand Name | Humulin R |
| Company | Eli Lilly and Company |
| Brand Discription | Humulin R(insulin human recombinant) U-100 is a polypeptide hormone structurally identical to human insulin synthesized through rDNA technology in a special non-disease producing laboratory strain of Escherichia coli bacteria. |
| Prescribed for | Treating diabetes mellitus. |
| Chemical Name | N.A. |
| Formulation | It contains human insulin (rDNA origin) 100 units/mL, glycerin 16 mg/mL and metacresol 2.5 mg/mL, endogenous zinc (approximately 0.015 mg/100 units) and water for injection. The pH is 7.0 to 7.8. Sodiumhydroxide and/or hydrochloric acid may be added durin |
| Physcial Appearance | Sterile, clear, aqueous, and colorless solution |
| Route of Administration | Subcutaneous Injection in the abdominal wall, the |
| Recommended Dosage | Humulin R (insulin (human recombinant)) U-100, when used subcutaneously, is usually given three or more times daily before meals. The average range of total daily insulin requirement for maintenance therapy in insulin-treated patients without severe insulin resistance lies between 0.5 and 1 unit/kg/day. |
| Contraindication | During episodes of hypoglycemia and in patients hypersensitive to humulin R. |
| Side Effects | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; wheezing; muscle pain; changes in vision; chills; confusion; dizziness; drowsiness; fainting; fast or irregular heartbeat; headache; loss of apetite. |
| Useful Link | http://www.drugs.com/cdi/humulin-r.html |
| PubMed ID | 22960692 |
| 3-D Structure | Th1027 (View) or (Download) |
| Entry 2 |
| (2) Primary information |
|---|
| ID | 1206 |
| ThPP ID | Th1027 |
| Therapeutic Peptide/Protein Name | Insulin Regular |
| Sequence | A-chain:GIVEQCCTSICSLYQLENYCN, B-chain:FVNQHLCGSHL view full sequnce in fasta |
| Functional Classification | Ia |
| Molecular Weight | 5.808 |
| Chemical Formula | C257H383N65O77S6 |
| Isoelectric Point | 5.39 |
| Hydrophobicity | 0.218 |
| Melting Point (℃) | 81 |
| Half Life | N.A. |
| Description | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. |
| Indication/Disease | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. |
| Pharmacodynamics | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. |
| Mechanism of Action | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. |
| Toxicity | Hypoglycemia is caused due to insulin toxicity. |
| Metabolism | Predominantly cleared by metabolic degradation via a receptor-mediated process. |
| Absorption | Generally well absorbed. |
| Volume of Distribution | 0.15 L/kg |
| Clearance | N.A. |
| Categories | Antidiabetic 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 | N.A. |
| Side Effects | N.A. |
| Useful Link | http://www.rxlist.com/humulin-r-drug.htm |
| PubMed ID | 22960692 |
| 3-D Structure | Th1027 (View) or (Download) |
| Entry 3 |
| (3) Primary information |
|---|
| ID | 1207 |
| ThPP ID | Th1027 |
| Therapeutic Peptide/Protein Name | Insulin Regular |
| Sequence | A-chain:GIVEQCCTSICSLYQLENYCN, B-chain:FVNQHLCGSHL view full sequnce in fasta |
| Functional Classification | Ia |
| Molecular Weight | 5.808 |
| Chemical Formula | C257H383N65O77S6 |
| Isoelectric Point | 5.39 |
| Hydrophobicity | 0.218 |
| Melting Point (℃) | 81 |
| Half Life | N.A. |
| Description | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. |
| Indication/Disease | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. |
| Pharmacodynamics | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. |
| Mechanism of Action | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. |
| Toxicity | Hypoglycemia is caused due to insulin toxicity. |
| Metabolism | Predominantly cleared by metabolic degradation via a receptor-mediated process. |
| Absorption | Generally well absorbed. |
| Volume of Distribution | 0.15 L/kg |
| Clearance | N.A. |
| Categories | Antidiabetic 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 | N.A. |
| Side Effects | N.A. |
| Useful Link | http://www.ncbi.nlm.nih.gov/pubmed/23512415 |
| PubMed ID | 22960692 |
| 3-D Structure | Th1027 (View) or (Download) |
| Entry 4 |
| (4) Primary information |
|---|
| ID | 1208 |
| ThPP ID | Th1027 |
| Therapeutic Peptide/Protein Name | Insulin Regular |
| Sequence | A-chain:GIVEQCCTSICSLYQLENYCN, B-chain:FVNQHLCGSHL view full sequnce in fasta |
| Functional Classification | Ia |
| Molecular Weight | 5.808 |
| Chemical Formula | C257H383N65O77S6 |
| Isoelectric Point | 5.39 |
| Hydrophobicity | 0.218 |
| Melting Point (℃) | 81 |
| Half Life | N.A. |
| Description | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. |
| Indication/Disease | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. |
| Pharmacodynamics | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. |
| Mechanism of Action | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. |
| Toxicity | Hypoglycemia is caused due to insulin toxicity. |
| Metabolism | Predominantly cleared by metabolic degradation via a receptor-mediated process. |
| Absorption | Generally well absorbed. |
| Volume of Distribution | 0.15 L/kg |
| Clearance | N.A. |
| Categories | Antidiabetic 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 | Novolin R |
| Company | Novo Nordisk |
| Brand Discription | Novolin R is a polypeptide hormone structurally identical to native human insulin and is produced by recombinant DNA technology, utilizing Saccharomyces cerevisiae(baker's yeast) as the production organism. |
| Prescribed for | Used for the treatment of patients with diabetes mellitus, for the control of hyperglycemia |
| Chemical Name | N.A. |
| Formulation | It contains human insulin (rDNA origin) 100 units/mL, glycerol 16 mg/mL, metacresol 3 mg/mL, zinc chloride approximately 7 mcg/mL and water for injection. The pH is adjusted to 7.4. Hydrochloric acid 2N or sodium hydroxide 2N may be added to adjust pH. No |
| Physcial Appearance | Sterile, clear, aqueous, and colorless solution |
| Route of Administration | Subcutaneous and Intravenous infusion |
| Recommended Dosage | The injection of Novolin R (recombinant dna origin) should be followed by a meal within approximately 30 minutes of administration The average range of total daily insulin requirement for maintenance therapy in insulin-treated patients lies between 0.5 and 1.0 IU/kg. |
| Contraindication | During episodes of hypoglycemia and in patients with hypersensitivity to Novolin R |
| Side Effects | Hypoglycemia, or low blood sugar, is the most common side effect. Symptoms include headache, hunger, dizziness, sweating, irritability, trouble concentrating, rapid breathing, fast heartbeat, fainting, or seizure (severe hypoglycemia can be fatal). |
| Useful Link | http://www.rxlist.com/novolin-r-drug.htm |
| PubMed ID | 22960692 |
| 3-D Structure | Th1027 (View) or (Download) |
| Entry 5 |
| (5) Primary information |
|---|
| ID | 1209 |
| ThPP ID | Th1027 |
| Therapeutic Peptide/Protein Name | Insulin Regular |
| Sequence | A-chain:GIVEQCCTSICSLYQLENYCN, B-chain:FVNQHLCGSHL view full sequnce in fasta |
| Functional Classification | Ia |
| Molecular Weight | 5.808 |
| Chemical Formula | C257H383N65O77S6 |
| Isoelectric Point | 5.39 |
| Hydrophobicity | 0.218 |
| Melting Point (℃) | 81 |
| Half Life | N.A. |
| Description | Insulin regular is a 51 residue peptide hormone, composed of two amino acid chains covalently linked by disulfide bonds. The structure is identical to native human insulin. Recombinant insulin is synthesized by recombinant DNA techncology. Inserting the human insulin gene into the Escherichia coli bacteria or Saccharomyces cerevisiae produces insulin for human use. |
| Indication/Disease | Indicated as an adjunct to diet and exercise to improve glycemic control in adults and children with type 1 and type 2 diabetes mellitus. |
| Pharmacodynamics | Insulin regular is a short-acting insulin. When subcutaneously administered, the onset of action (as evidenced by a decrease in glucose level) occurs 30 minutes post-dose. Maximal effect occurs between 1.5 and 3.5 hours post-dose. The glucose-lowering effect occurs 8 hours post-dose. Compared to other rapid-acting insulin analogs, insulin regular has a slower onset of action and longer duration of action. |
| Mechanism of Action | The primary activity of insulin is the regulation of glucose metabolism. Insulin promotes glucose and amino acid uptake into muscle and adipose tissues, and other tissues except brain and liver. It also has an anabolic role in stimulating glycogen, fatty acid, and protein synthesis. Insulin inhibits gluconeogenesis in the liver. Insulin binds to the insulin receptor (IR), a heterotetrameric protein consisting of two extracellular alpha units and two transmembrane beta units. The binding of insulin to the alpha subunit of IR stimulates the tyrosine kinase activity intrinsic to the beta subunit of the receptor. The bound receptor is able to autophosphorylate and phosphorylate numerous intracellular substrates such as insulin receptor substrates (IRS) proteins, Cbl, APS, Shc and Gab 1. These activated proteins, in turn, lead to the activation of downstream signaling molecules including PI3 kinase and Akt. Akt regulates the activity of glucose transporter 4 (GLUT4) and protein kinase C (PKC) which play a critical role in metabolism and catabolism. |
| Toxicity | Hypoglycemia is caused due to insulin toxicity. |
| Metabolism | Predominantly cleared by metabolic degradation via a receptor-mediated process. |
| Absorption | Generally well absorbed. |
| Volume of Distribution | 0.15 L/kg |
| Clearance | N.A. |
| Categories | Antidiabetic 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 | N.A. |
| Side Effects | N.A. |
| Useful Link | http://www.drugs.com/mtm/novolin-r.html |
| PubMed ID | 22960692 |
| 3-D Structure | Th1027 (View) or (Download) |