Toxicological Research

  • 제21권4호
  • /
  • Pages.319-323
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  • 2005
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  • 1976-8257(pISSN)
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  • 2234-2753(eISSN)
한국독성학회 (Korean Society of Toxicology & Korea Environmental Mutagen Society)
권호 표지

Systemic Availability and Pharmacokinetics of Surfactin, a Lipopeptide Produced by Bacillus subtilis BC1212 in Rats

  • Lim Jong-Hwan (B&C Biopharm) ;
  • Kim Myoung-Seok (College of Veterinary Medicine, Chungnam National University) ;
  • Park Byung-Kwon (College of Veterinary Medicine, Chungnam National University) ;
  • Hwang Youn-Hwan (College of Veterinary Medicine, Chungnam National University) ;
  • Hwang Mi-Hyun (College of Veterinary Medicine, Kyoungbuk National University) ;
  • Park Seung-Chun (College of Veterinary Medicine, Kyoungbuk National University) ;
  • Yun Hyo-In (College of Veterinary Medicine, Chungnam National University)
  • 발행 : 2005.12.01
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초록

The aim of the present study was to evaluate systemic bioavailability of surfactin and to determine its pharmacokinetic profiles. The stability of surfactin to pH, temperature and protease was evaluated. Surfactin was resistant to high temperature, a wide range of pH and the action of hydrolytic enzymes. The pharmacokinetic natures of surfactin which were shown the short half-life, rapid clearance and poor bioavailability. The results of study should provide preliminary data of surfactin for further dose-finding studies and for the design of application forms. It is also be important to a context of the safety of surfactin.

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참고문헌

  1. Arima, K., Kakinuma, A. and Tamura, G. (1968): Surfactin, a crystalline peptidelipid surfactant produced by Bacillus subtilis: isolation, characterization and its inhibition of fibrin clot formation. Biochem. Biophys. Res. Commun., 31, 488-494 https://doi.org/10.1016/0006-291X(68)90503-2
  2. Baumgart, F., Kluge, B., Ullrich, C., Vater, J. and Ziessow, D. (1991): Identification of amino acid substitutions in the lipopeptide surfactin using 2D NMR spectroscopy. Biochem. Biophys. Res. Commun., 177, 998-1005 https://doi.org/10.1016/0006-291X(91)90637-M
  3. Bonmatin, J.M., Genest, M., Labbe, H. and Ptak, M. (1994): Solution three-dimensional structure of surfactin: a cyclic lipopeptide studied by 1H-NMR, distance geometry, and molecular dynamics. Biopolymers, 34, 975-986 https://doi.org/10.1002/bip.360340716
  4. Donoso, G., Craig, G.O. and Baldwin, R.S. (1970): The distribution and excretion of zinc $bacitracin-^{14}C$ in rats and swine. Toxicol. Appl. Pharmacol., 17, 366-374 https://doi.org/10.1016/0041-008X(70)90194-8
  5. Desai, J.D. and Banat, I.M. (1997): Microbial production of surfactants and their commercial potential. Microbiol. Mol. Biol. Rev., 61, 47-64
  6. Froyshov, O., Pedersen, S. and Hove, K. (1986): Absorption, metabolism and excretion of zinc $C^{14}$-bacitracin fed to young pigs. J. Anim. Physiol. Anim. Nutr., 55, 100-110 https://doi.org/10.1111/j.1439-0396.1986.tb00706.x
  7. Grangemard, I., Bonmatin, J.M., Bernillon, J., Das, B.C. and Peypoux, F. (1999): Lichenysins G, a novel family of lipopeptide biosurfactants from Bacillus licheniformis 1M 1307: production, isolation and structural evaluation by NMR and mass spectrometry. J. Antibiot., 52, 363-373 https://doi.org/10.7164/antibiotics.52.363
  8. Hamman, J.H., Enslin, G.M. and Kotze, A.F. (2005): Oral delivery of peptide drugs: barriers and developments. BioDrugs, 19, 165-177 https://doi.org/10.2165/00063030-200519030-00003
  9. Kikuchi, T. and Hasumi, K. (2002): Enhancement of plasminogen activation by surfactin C: augmentation of fibrinolysis in vitro and in vivo. Biochim. Biophys. Acta, 1596, 234-245
  10. Kanatomo, S., Nagai, S., Ohki, K. and Yasuda, Y. (1995): Study on surfactin, a cyclic depsipeptide. I. Isolation and structure of eight surfuctin analogs produced by Bacillus natto KMD2311. Yakugaku Zasshi, 115, 756-764 https://doi.org/10.1248/yakushi1947.115.9_756
  11. Kowall, M., Vater, J., Kluge, B., Stein, T., Franke, P. and Ziessow, D. (1998): Separation and characterization of surfactin isoforms produced by Bacillus subtilis OKB-105. J. Colloid. Interface Sci., 204, 1-8 https://doi.org/10.1006/jcis.1998.5558
  12. LeCluyse, E.L. and Sutton, S.C. (1997): In vitro models for selection of development candidates. Permeability studies to define mechanisms of absorption enhancement. Adv. Drug Deliv. Rev., 23, 163-183 https://doi.org/10.1016/S0169-409X(96)00434-6
  13. Lee, V.H.L. (1990): Protease inhibitors and penetration enhancers as approaches to modify peptide absorption. J. Control Release, 13, 213-223 https://doi.org/10.1016/0168-3659(90)90011-H
  14. Peypoux, F., Bonmatin, J.M. and Wallach, J. (1999): Recent trends in the biochemistry of surfactin. Appl. Microbiol. Biotechnol., 51, 553-563 https://doi.org/10.1007/s002530051432
  15. Sullivan, E.R. (1985): Molecular genetics of biosurfactants production. Curr. Opin. Biotechno., 9, 263-269
  16. Singh, P. and Cameotra, S.S. (2004): Potential applications of microbial surfactants in biomedical sciences. Trends Biotechnol., 22, 142-146 https://doi.org/10.1016/j.tibtech.2004.01.010
  17. Vollenbroich, D., Ozel, M., Vater, J., Kamp, R.M. and Pauli, G. (1997a): Mechanism of inactivation of enveloped viruses by the biosurfactant surfactin from Bacillus subtilis. Biologicals, 25, 289-297 https://doi.org/10.1006/biol.1997.0099
  18. Vollenbroich, D., Pauli, G., Ozel, M. and Vater, J. (1997b): Antimycoplasma properties and application in cell culture of surfactin, a Iipopeptide antibiotic from Bacillus subtilis. Appl. Environ. Microbiol., 63, 44-49