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Showing drug card for Botulinum Toxin Type A (DB00083)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:26
Primary Accession Number DB00083
Secondary Accession Number
  • BIOD00092
  • BTD00092
Name Botulinum Toxin Type A
Drug Type
  • Approved
  • Biotech
  • Investigational
Description Purified botulinum toxin from Clostridium botulinum, purified from culture via dialysis and acid precipitation.
Synonyms
  1. BTX-A
  2. BoNT/A
  3. Bontoxilysin A
  4. Botulinum neurotoxin type A precursor
  5. botulinum toxin type A
Brand Names
  1. BOTOX (Allegran Inc)
  2. BOTOX Cosmetic (Allegran Inc)
  3. Botox
  4. Dysport
Brand Mixtures Not Available
Chemical IUPAC Name Not Available
Chemical Formula C6760H10447N1743O2010S32
Chemical Structure Structure
Protein Sequence(s) >DB00083 sequence 
PFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNP
PPEAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGS
TIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYG
STQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNR
VFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAK
SIVGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVL
NRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTG
LFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEI
TSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGK
KYELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAA
MFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGA
VILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKV
NTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAM
ININKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKV
NNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIG
SKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNE
YTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITN
NRLNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNE
KEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRG
SVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAG
VEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKL
VASNWYNRQIERSSRTLGCSWEFIPVDDGWGERPL
CAS Registry Number 93384-43-1
InChI Identifier Not Available
InChI Key Not Available
KEGG Drug D00783 Link Image
KEGG Compound C07946 Link Image
PubChem Compound Not Available
PubChem Substance 7847848 Link Image
ChEBI ID Not Available
PharmGKB ID PA448659 Link Image
HET ID Not Available
GenBank ID X52066 Link Image
Drug ID Number [DIN] 02243721 Link Image
RxList Link http://www.rxlist.com/cgi/generic/botox.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Botox Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 149322.7000
Monoisotopic Molecular Weight Not Available
State Solid
Melting Point Not Available
Experimental Water Solubility Soluble Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.368 Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point 6.06
Mass Spectrum Not Available
MOL File Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID 3BTA Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category
  • Anti-Wrinkle Agents
  • Antidystonic Agents
  • Neuromuscular Blocking Agents
ATC Codes
AHFS Codes
  • 92:00.00
Indication For the treatment of cervical dystonia in adults to decrease the severity of abnormal head position and neck pain associated with cervical dystonia. Also for the treatment of severe primary axillary hyperhidrosis that is inadequately managed with topical agents and for the treatment of strabismus and blepharospasm associated with dystonia, including benign essential blepharospasm or VII nerve disorders in patients 12 years of age and above. Also used cosmetically to temporarily improve the appearance of moderate-to-severe frown lines between the eyebrows (glabellar lines) as well as for the treatment of excessive underarm sweating.
Pharmacology A 150 kDa neurotoxic protein produced from fermentation of Hall strain Clostridium botulinum type A grown in a medium containing casein hydrolysate, glucose and yeast extract. It is purified from the culture solution by dialysis and a series of acid precipitations to a complex consisting of the neurotoxin, and several accessory proteins. Botulinum Toxin Type A is not expected to be present in the peripheral blood at measurable levels following IM or intradermal injection at the recommended doses. The recommended quantities of neurotoxin administered at each treatment session are not expected to result in systemic, overt distant clinical effects, i.e. muscle weakness, in patients without other neuromuscular dysfunction. However, sub-clinical systemic effects have been shown by single-fiber electromyography after IM doses of botulinum toxins appropriate to produce clinically observable local muscle weakness.
Mechanism of Action Botulinum Toxin Type A blocks neuromuscular transmission by binding to acceptor sites on motor or sympathetic nerve terminals, entering the nerve terminals, and inhibiting the release of acetylcholine. This inhibition occurs as the neurotoxin cleaves SNAP-25, a protein integral to the successful docking and release of acetylcholine from vesicles situated within nerve endings.
Absorption The chemical complexity of Botulinum Toxin Type A combined with its extreme potency limits the opportunity to study its pharmacokinetic profile in humans. Therefore, no human pharmacokinetic studies have been performed. Botulinum Toxin Type A is injected directly into the target organ, a skeletal muscle. Thus, bioavailability of the intravenous or oral route is not of clinical relevance.
Toxicity Based on toxicological studies, it has been estimated that the human LD50 by injection is approximately 2800 Units, equivalent to 28 individual vials of BOTOX (Botulinum Toxin Type A) Purified Neurotoxin Complex (100 Units) for a 70 kg adult. When injected intramuscularly, Botulinum Toxin Type A has been shown to be teratogenic or to have embryocidal effects in some animal species.
Protein Binding Not Available
Biotransformation Not Available
Half Life Not Available
Dosage Forms
Form Route
Powder, for solution Intramuscular
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Brin MF, Lew MF, Adler CH, Comella CL, Factor SA, Jankovic J, O'Brien C, Murray JJ, Wallace JD, Willmer-Hulme A, Koller M: Safety and efficacy of NeuroBloc (botulinum toxin type B) in type A-resistant cervical dystonia. Neurology. 1999 Oct 22;53(7):1431-8. [PubMed Link Image]
  2. Shukla HD, Sharma SK: Clostridium botulinum: a bug with beauty and weapon. Crit Rev Microbiol. 2005;31(1):11-8. [PubMed Link Image]
  3. Eisenach JH, Atkinson JL, Fealey RD: Hyperhidrosis: evolving therapies for a well-established phenomenon. Mayo Clin Proc. 2005 May;80(5):657-66. [PubMed Link Image]
  4. Montecucco C, Molgo J: Botulinal neurotoxins: revival of an old killer. Curr Opin Pharmacol. 2005 Jun;5(3):274-9. [PubMed Link Image]
  5. Schurch B, Corcos J: Botulinum toxin injections for paediatric incontinence. Curr Opin Urol. 2005 Jul;15(4):264-7. [PubMed Link Image]
  6. Wikipedia Link Image
  7. RxList Link Image
Organisms Affected
  • Humans and other mammals
Targets
  1. Synaptosomal-associated protein 25
Drug Target 1 [top]
Target 1 ID 433
Target 1 Name Synaptosomal-associated protein 25
Target 1 Synonyms
  1. SNAP-25
  2. SUP
  3. Super protein
  4. Synaptosomal-associated 25 kDa protein
Target 1 Gene Name SNAP25
Target 1 Protein Sequence >Synaptosomal-associated protein 25 
MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERI
EEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARV
VDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDR
IMEKADSNKTRIDEANQRATKMLGSG
Target 1 Number of Residues 209
Target 1 Molecular Weight 23315
Target 1 Theoretical pI 4.39
Target 1 GO Classification Not Available
Target 1 General Function Involved in regulation of insulin secretion
Target 1 Specific Function t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 307426 Link Image
Target 1 UniProtKB/Swiss-Prot ID P60880 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name SNP25_HUMAN Link Image
Target 1 PDB ID 1SFC Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location Not Available
Target 1 Gene Sequence >621 bp 
ATGGCCGAAGACGCAGACATGCGCAATGAGCTGGAGGAGATGCAGCGAAGGGCTGACCAG
TTGGCTGATGAGTCGCTGGAAAGCACCCGTCGTATGCTGCAACTGGTTGAAGAGAGTAAA
GATGCTGGTATCAGGACTTTGGTTATGTTGGATGAACAAGGAGAACAACTCGATCGTGTC
GAAGAAGGCATGAACCATATCAACCAAGACATGAAGGAGGCTGAGAAAAATTTAAAAGAT
TTAGGGAAATGCTGTGGCCTTTTCATATGTCCTTGTAACAAGCTTAAATCAAGTGATGCT
TACAAAAAAGCCTGGGGCAATAATCAGGATGGAGTGGTGGCCAGCCAGCCTGCTCGTGTA
GTGGACGAACGGGAGCAGATGGCCATCAGTGGCGGCTTCATCCGCAGGGTAACAAATGAT
GCCCGAGAAAATGAAATGGATGAAAACCTAGAGCAGGTGAGCGGCATCATCGGGAACCTC
CGTCACATGGCCCTGGATATGGGCAATGAGATCGATACACAGAATCGCCAGATCGACAGG
ATCATGGAGAAGGCTGATTCCAACAAAACCAGAATTGATGAGGCCAACCAACGTGCAACA
AAGATGCTGGGAAGTGGTTAA
Target 1 GenBank Gene ID
Target 1 GeneCard ID SNAP25 Link Image
Target 1 GenAtlas ID SNAP25 Link Image
Target 1 HGNC ID HGNC:11132 Link Image
Target 1 Chromosome Location 20
Target 1 Locus 20p12-p11.2
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Chen X, Tomchick DR, Kovrigin E, Arac D, Machius M, Sudhof TC, Rizo J: Three-dimensional structure of the complexin/SNARE complex. Neuron. 2002 Jan 31;33(3):397-409. [PubMed Link Image]
  3. Zhao N, Hashida H, Takahashi N, Sakaki Y: Cloning and sequence analysis of the human SNAP25 cDNA. Gene. 1994 Aug 5;145(2):313-4. [PubMed Link Image]
  4. Bark IC, Wilson MC: Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25. Gene. 1994 Feb 25;139(2):291-2. [PubMed Link Image]
  5. Jagadish MN, Fernandez CS, Hewish DR, Macaulay SL, Gough KH, Grusovin J, Verkuylen A, Cosgrove L, Alafaci A, Frenkel MJ, Ward CW: Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. Biochem J. 1996 Aug 1;317 ( Pt 3):945-54. [PubMed Link Image]
Target 1 Drug References
  1. Zhou JY, Wang ZF, Ren XM, Tang MZ, Shi YL: Antagonism of botulinum toxin type A-induced cleavage of SNAP-25 in rat cerebral synaptosome by toosendanin. FEBS Lett. 2003 Dec 4;555(2):375-9. [PubMed Link Image]
  2. Flynn TC: Myobloc. Dermatol Clin. 2004 Apr;22(2):207-11, vii. [PubMed Link Image]
  3. Okada M, Yoshida S, Zhu G, Kaneko S: [Methodological consideration in studying the exocytosis mechanisms using microdialysis] Nihon Shinkei Seishin Yakurigaku Zasshi. 2004 Aug;24(4):165-70. [PubMed Link Image]
  4. Frassoni C, Inverardi F, Coco S, Ortino B, Grumelli C, Pozzi D, Verderio C, Matteoli M: Analysis of SNAP-25 immunoreactivity in hippocampal inhibitory neurons during development in culture and in situ. Neuroscience. 2005;131(4):813-23. [PubMed Link Image]
  5. Straughan D: Progress in applying the Three Rs to the potency testing of Botulinum toxin type A. Altern Lab Anim. 2006 Jun;34(3):305-13. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.