Borrelidin molecular structure

Borrelidin is a nitrile-containing 18-membered macrolide antibiotic produced by Streptomyces rochei and related species. It functions as a highly selective inhibitor of threonyl-tRNA synthetase (ThrRS) in both prokaryotic and eukaryotic systems, thereby disrupting protein synthesis. In addition to its broad-spectrum antimicrobial activity, borrelidin exhibits potent antiangiogenic effects (IC₅₀ ≈ 0.8 nM), induces apoptosis in endothelial cells, and shows antimalarial and anticancer potential. Its unique structure and multifunctional bioactivity make it a valuable tool in antibiotic research, angiogenesis studies, and drug discovery.

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*FOR RESEARCH USE ONLY. Not for human or veterinary use. This product is intended exclusively for laboratory research and must not be used in diagnostic or therapeutic applications.


Borrelidin Specifications

Production strain Streptomyces parvulus
Formula C₂₈H₄₃NO₆
Purity ≥98%
Solubility Soluble in methanol, chloroform, and DMSO
Storage Temperature -
Shipping Temperature ambient
SMILES O=C1C[C@H](O)[C@@H](C)C[C@@H](C)C[C@@H](C)C[C@H](C)[C@@H](O)/C(C#N)=C\C=C\C[C@]([C@]2([H])CCC[C@H]2C(O)=O)([H])O1
CAS Number 7184-60-3
Synonyms (1R)-2R-[7-cyano-8R,16S-dihydroxy-9S,11R,13S,15S-tetramethyl-18-oxooxacyclooctadeca-4E,6Z-dien-2S-yl]-cyclopentanecarboxylic acid;NSC216128;treponemycin
  • Woolard, J., Vousden, W., Moss, S. J., Krishnakumar, A., Gammons, M. V., Nowak, D. G., Dixon, N., Micklefield, J., Spannhoff, A., Bedford, M. T., Gregory, M. A., Martin, C. J., Leadlay, P. F., Zhang, M. Q., Harper, S. J., Bates, D. O., & Wilkinson, B. (2011). Borrelidin modulates the alternative splicing of VEGF in favour of anti-angiogenic isoforms. Chemical science, 2011(2), 273–278. https://doi.org/10.1039/C0SC00297F
  • Kawamura, T., Liu, D., Towle, M. J., Kageyama, R., Tsukahara, N., Wakabayashi, T., & Littlefield, B. A. (2003). Anti-angiogenesis effects of borrelidin are mediated through distinct pathways: threonyl-tRNA synthetase and caspases are independently involved in suppression of proliferation and induction of apoptosis in endothelial cells. The Journal of antibiotics, 56(8), 709–715. https://doi.org/10.7164/antibiotics.56.709
  • Otoguro, K., Ui, H., Ishiyama, A., Kobayashi, M., Togashi, H., Takahashi, Y., Masuma, R., Tanaka, H., Tomoda, H., Yamada, H., & Omura, S. (2003). In vitro and in vivo antimalarial activities of a non-glycosidic 18-membered macrolide antibiotic, borrelidin, against drug-resistant strains of Plasmodia. The Journal of antibiotics, 56(8), 727–729. https://doi.org/10.7164/antibiotics.56.727
  • Tsuchiya, E., Yukawa, M., Miyakawa, T., Kimura, K. I., & Takahashi, H. (2001). Borrelidin inhibits a cyclin-dependent kinase (CDK), Cdc28/Cln2, of Saccharomyces cerevisiae. The Journal of antibiotics, 54(1), 84–90. https://doi.org/10.7164/antibiotics.54.84
  • Wilkinson, B., Gregory, M. A., Moss, S. J., Carletti, I., Sheridan, R. M., Kaja, A., Ward, M., Olano, C., Mendez, C., Salas, J. A., Leadlay, P. F., vanGinckel, R., & Zhang, M. Q. (2006). Separation of anti-angiogenic and cytotoxic activities of borrelidin by modification at the C17 side chain. Bioorganic & medicinal chemistry letters, 16(22), 5814–5817. https://doi.org/10.1016/j.bmcl.2006.08.073
  • Mirando, A. C., Fang, P., Williams, T. F., Baldor, L. C., Howe, A. K., Ebert, A. M., Wilkinson, B., Lounsbury, K. M., Guo, M., & Francklyn, C. S. (2015). Aminoacyl-tRNA synthetase dependent angiogenesis revealed by a bioengineered macrolide inhibitor. Scientific reports, 5, 13160. https://doi.org/10.1038/srep13160
Need additional documentation? Safety Data Sheet, Certificate of Analysis and batch-specific data are available upon request from our technical support team.

Our Borrelidin Prices

*For custom handling, including aliquoting or specific packaging formats, please get in touch with our technical support team.
QuantityCost
100 µg $85
1 mg $181
5 mg $440
10 mg $566
>10 mg Request a Quote
💡 Bulk Discounts Available: Contact us for custom pricing on orders over 10 mg

Isomerase

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