The Science of Botox

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BOTOX® Cosmetic (onabotulinumtoxinA) is a purified protein derived from the bacterium Clostridium botulinum.¹ Botulinum toxins have been studied for more than 100 years.

In the late 1890s, scientists first identified C. botulinum as a cause of food poisoning (botulism). Scientists continued to study its effects, exploring its therapeutic uses in the late 1960s.² By 1989, BOTOX® (onabotulinumtoxinA) was approved for medical use.³ The same product with dosing specific to glabellar lines was approved as BOTOX® Cosmetic in 2002.

The BOTOX® Cosmetic formulation

In nature, the botulinum neurotoxin associates with complementary nontoxic accessory proteins to produce protein complexes.4,5

The role of accessory proteins

Studies show botulinum neurotoxin type A accessory proteins help stabilize the core neurotoxin against thermal and pH stress.6,7 BOTOX® Cosmetic includes these protective proteins.

 Biologics are inherently unique

Biological products (biologics), like botulinum toxins, are inherently unique and cannot be easily replicated:

Changes in manufacturing could result in changes to the biological molecule that could profoundly alter the efficacy or safety profile9




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1. BOTOX® Cosmetic Prescribing Information, November 2011.
2. Schantz EJ, Johnson EA. Botulinum toxin: The story of its development for the treatment of human disease. Perspect Biol Med.1997;40(3):317-327.
3. US Food and Drug Administration. List of Orphan Products Designated and Approved as of December 31, 2003. US Food and Drug Administration website. Accessed February 22, 2012
4. Inoue K, Fujinaga Y, Watanabe T, et al. Molecular composition of Clostridium botulinum type A progenitor toxins. Infect Immun. 1996;64(5):1589-1594.
5. Ohishi I, Sugii S, Sakaguchi G. Oral toxicities of Clostridium botulinum toxins in response to molecular size. Infect Immun. 1977;16(1):107-109.
6. Brandau DT, Joshi SB, Smalter AM, et al. Stability of the Clostridium botulinum type A neurotoxin complex: an empirical phase diagram based approach. Mol Pharm. 2007;4(4):571-582.
7. Kukreja RV, Singh BR. Compara¬tive role of neurotoxin-associated proteins in the structural stability and endopeptidase activity of botulinum neurotoxin complex types A and E. Biochemistry. 2007;46(49):14316-14324.
8. Lietzow MA, Gielow ET, Le D, Zhang J, Verhagen MF. Subunit stoichiometry of the Clostridium botulinum type A neurotoxin complex determined using denaturing capillary electrophoresis. Protein J. 2008;27(7-8):420-425.
9. Roger SD, Mikhail A. Biosimilars: opportunity or cause for concern? J Pharm Pharm Sci. 2007;10(3):405-410.