A database of FDA approved therapeutic peptides and proteins
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1206 details |
Primary information | |
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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 Appearnce | 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) |