A database of FDA approved therapeutic peptides and proteins
Details of Th1042 which contains 17 entries. |
Entry 1 | |
(1) Primary information | |
---|---|
ID | 1288 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | N.A. |
Target | Collagen alpha-1(I) chain,Collagen alpha-1(II) chain,Collagen alpha-1(III) chain,Collagen alpha-2(I) chain |
Information of corresponding available drug in the market | |
Brand Name | Cordase |
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.lantus.com/considering/lantus-solostar-features/lantus-solostar-pen |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 2 | |
(2) Primary information | |
---|---|
ID | 1289 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Grafco Silver Nitrate (silver nitrate topical) |
Target | N.A. |
Information of corresponding available drug in the market | |
Brand Name | Santyl |
Company | Advance Biofactures Corp |
Brand Discription | Collagenase Santyl ointment is a sterile enzymatic debriding ointment which contains 250 collagenase units per gram of white petrolatum USP. The enzyme collagenase is derived from the fermentation by Clostridium histolyticum. It possesses the unique abili |
Prescribed for | Used to remove dead skin from wounds and burned areas. Santyl ointment is an enzymatic debriding ointment which works by breaking down dead skin. |
Chemical Name | N.A. |
Formulation | Collagenase Santyl Ointment contains 250 units of collagenase enzyme per gram of white petrolatum USP. The potency assay of collagenase is based on the digestion of undenatured collagen (from bovine Achilles tendon) at pH 7.2 and 37°C for 24 hours. The nu |
Physcial Appearance | Sterile enzymatic debriding ointment |
Route of Administration | Apply on the affected area. |
Recommended Dosage | Collagenase Santyl Ointment should be applied once daily (or more frequently if the dressing becomes soiled as from incontinence). |
Contraindication | Hypersensitivity |
Side Effects | Rash; hives; itching; difficulty breathing; tightness in the chest; swelling of the mouth, face, lips, or tongue; signs of infection (eg, fever, chills, or persistent sore throat). |
Useful Link | http://www.santyl.com |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 3 | |
(3) Primary information | |
---|---|
ID | 1290 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | SilvrSTAT (silver topical) |
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/santyl-drug.htm |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 4 | |
(4) Primary information | |
---|---|
ID | 1291 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Thermazene (silver sulfadiazine topical) |
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/cdi/santyl-ointment.html |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 5 | |
(5) Primary information | |
---|---|
ID | 1292 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | silver / zinc oxide topical |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 6 | |
(6) Primary information | |
---|---|
ID | 1293 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | SilvaSorb (silver topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 7 | |
(7) Primary information | |
---|---|
ID | 1294 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Mersol (thimerosal topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 8 | |
(8) Primary information | |
---|---|
ID | 1295 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | silver sulfadiazine topical |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 9 | |
(9) Primary information | |
---|---|
ID | 1296 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | SSD AF (silver sulfadiazine topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 10 | |
(10) Primary information | |
---|---|
ID | 1297 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Silvadene Cream 1% (silver sulfadiazine topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 11 | |
(11) Primary information | |
---|---|
ID | 1298 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | Silvadene (silver sulfadiazine topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 12 | |
(12) Primary information | |
---|---|
ID | 1299 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | SSD (silver sulfadiazine topical) |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 13 | |
(13) Primary information | |
---|---|
ID | 1300 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | silver nitrate topical |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 14 | |
(14) Primary information | |
---|---|
ID | 1301 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
Patents Number | N.A. |
Date of Issue | N.A. |
Date of Expiry | N.A. |
Drug Interaction | thimerosal topical |
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 | N.A. |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 15 | |
(15) Primary information | |
---|---|
ID | 1302 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
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 | Xiaflex |
Company | Auxilium |
Brand Discription | It contains purified collagenase clostridium histolyticum, consisting of two microbial collagenases in a defined mass ratio, Collagenase AUX-I and Collagenase AUX-II, which are isolated and purified from the fermentation of Clostridium histolyticum bacter |
Prescribed for | XIAFLEX is indicated for the treatment of adult patients with Dupuytren's contracture with a palpable cord. XIAFLEX is also indicated for the treatment of adult men with Peyronie's disease with a palpable plaque and curvature deformity of at least 30 degr |
Chemical Name | N.A. |
Formulation | XIAFLEX is available in single-use, glass vials containing 0.9 mg of collagenase clostridium histolyticum. Each vial also contains 0.5 mg of hydrochloric acid, 18.5 mg of sucrose, and 1.1 mg of tromethamine. |
Physcial Appearance | Sterile lyophilized powder (white cake) and must be reconstituted with the provided diluent prior to use. |
Route of Administration | Intralesional Injection |
Recommended Dosage | The dose of XIAFLEX is 0.58 mg per injection into a palpable cord with a contracture of a metacarpophalangeal (MP) joint or a proximal interphalangeal (PIP) joint |
Contraindication | The treatment of Peyronie's plaques that involve the penile urethra due to potential risk to this structure. |
Side Effects | Swelling, bruising, or bleeding where the medicine was injected; mild pain or tenderness in the treated hand; swollen glands in your elbow or underarm; itching, redness, or warmth of the skin; cracked skin; or underarm pain. |
Useful Link | https://www.xiaflex.com |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 16 | |
(16) Primary information | |
---|---|
ID | 1303 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
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 | Patients with a history of hypersensitivity to XIAFLEX or to collagenase used in any other therapeutic application or application method |
Side Effects | N.A. |
Useful Link | http://www.drugs.com/xiaflex.html |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |
Entry 17 | |
(17) Primary information | |
---|---|
ID | 1304 |
ThPP ID | Th1042 |
Therapeutic Peptide/Protein Name | Collagenase |
Sequence | MKRKCLSKRLMLAITMATIFTVNSTLPIYAAVDKNNATAAVQNESKRYTV view full sequnce in fasta |
Functional Classification | Ic |
Molecular Weight | 112023.2 |
Chemical Formula | C5028H7666N1300O1564S21 |
Isoelectric Point | 5.58 |
Hydrophobicity | -0.714 |
Melting Point (℃) | N.A. |
Half Life | N.A. |
Description | This enzyme is derived from fermentation of Clostridium histolyticum |
Indication/Disease | It promotes debridement of necrotic tissue and helps in the treatment of severe burns and dermal ulcers including decubitus ulcers. |
Pharmacodynamics | Helps in the treatment of skin ulcers and severe burns, collagenase is able to digest collagen in necrotic tissue at physiological pH by hydrolyzing the peptide bonds of undenatured and denatured collagen. Collagenase thus contributes towards the formation of granulation tissue and subsequent epithelization of dermal ulcers and severely burned areas. The action of collagenase may remove substrates necessary for bacterial proliferation or may permit antibodies, leukocytes, and antibiotics better access to the infected area. |
Mechanism of Action | Collagenase is a protease that is specific to collagen. The triple helical region of interstitial collagens is highly resistant to most cell proteinases. However, during remodeling of the connective tissue in such processes as wound healing and metastasis, collagen becomes susceptible to cleavage by collagenases. Collagenase cleaves all 3 alpha helical chains of native Types I, II and III collagens at a single locus by hydrolyzing the peptide bond following the Gly residue of the sequence: Gly 775-(Ile or Leu) 776-(Ala or Leu) 777 located approximately three-fourths of the chain length from each N-terminus. |
Toxicity | N.A. |
Metabolism | N.A. |
Absorption | N.A. |
Volume of Distribution | N.A. |
Clearance | N.A. |
Categories | N.A. |
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/xiaflex-drug.htm |
PubMed ID | 11937475 |
3-D Structure | Th1042 (View) or (Download) |