Jasplakinolide

Jasplakinolide
Names
	IUPAC name Cyclo[(3R)-3-(4-hydroxyphenyl)-β-alanyl-(2S,4E,6R,8S)-8-hydroxy-2,4,6-trimethyl-4-nonenoyl-L-alanyl-2-bromo-N-methyl-D-tryptophyl]
Identifiers
CAS Number	102396-24-7;
3D model (JSmol)	Interactive image;
ChEMBL	ChEMBL257166;
ChemSpider	52563404;
KEGG	C16883;
PubChem CID	9831636;
	InChI InChI=1S/C36H45BrN4O6/c1-20-15-21(2)17-23(4)47-32(43)19-30(25-11-13-26(42)14-12-25)40-35(45)31(18-28-27-9-7-8-10-29(27)39-33(28)37)41(6)36(46)24(5)38-34(44)22(3)16-20/h7-15,21-24,30-31,39,42H,16-19H2,1-6H3,(H,38,44)(H,40,45)/b20-15+/t21-,22-,23-,24-,30+,31+/m0/s1 Key: GQWYWHOHRVVHAP-DHKPLNAMSA-N;
	SMILES C[C@@H]\1C[C@@H](OC(=O)C[C@@H](NC(=O)[C@H](N(C(=O)[C@@H](NC(=O)[C@H](C/C(=C1)/C)C)C)C)CC2=C(NC3=CC=CC=C32)Br)C4=CC=C(C=C4)O)C;
	Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). Infobox references

Jasplakinolide is a naturally occurring cyclo-depsipeptide. It was first isolated from a species of marine sponge named Jaspis johnstoni. It is permeable to the cell membrane meaning that it is able to cross the membrane.^[1] Once it crosses the cell membrane, it is a potent inducer and stabilizer of actin filaments meaning that it rapidly stabilizes pre-existing filaments and polymerize the protein actin.^[2] It also inhibits the disassembly of theses filaments. When doing this, it competes with Phalloidin making it unable to bind with F-actin.^[3]

Applications

Jasplakinolide is potentially important in medical applications showing anti-cancer, fungicidal and antiproliferative properties. It also has important scientific applications for the study of organelles, and actin filaments.^[1]^[2]^[4]

References

^ ^a ^b Holzinger, Andreas (2009). "Jasplakinolide: an actin-specific reagent that promotes actin polymerization". Cytoskeleton Methods and Protocols. Methods in Molecular Biology (Clifton, N.J.). Vol. 586. pp. 71–87. doi:10.1007/978-1-60761-376-3_4. ISBN 978-1-60761-375-6. ISSN 1940-6029. PMID 19768425.
^ ^a ^b Bubb, Michael R.; Spector, Ilan; Beyer, Bret B.; Fosen, Katina M. (2000-02-18). "Effects of Jasplakinolide on the Kinetics of Actin Polymerization: AN EXPLANATION FOR CERTAIN IN VIVO OBSERVATIONS*". Journal of Biological Chemistry. 275 (7): 5163–5170. doi:10.1074/jbc.275.7.5163. ISSN 0021-9258. PMID 10671562.
^ "Jasplakinolide | Actin Polymerization Inducer | MedChemExpress". MedchemExpress.com. Retrieved 2025-08-02.
^ Bubb, M. R.; Senderowicz, A. M.; Sausville, E. A.; Duncan, K. L.; Korn, E. D. (1994-05-27). "Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin". Journal of Biological Chemistry. 269 (21): 14869–14871. doi:10.1016/S0021-9258(17)36545-6. ISSN 0021-9258. PMID 8195116.

[:0-1] Holzinger, Andreas (2009). "Jasplakinolide: an actin-specific reagent that promotes actin polymerization". Cytoskeleton Methods and Protocols. Methods in Molecular Biology (Clifton, N.J.). Vol. 586. pp. 71–87. doi:10.1007/978-1-60761-376-3_4. ISBN 978-1-60761-375-6. ISSN 1940-6029. PMID 19768425.

[:1-2] Bubb, Michael R.; Spector, Ilan; Beyer, Bret B.; Fosen, Katina M. (2000-02-18). "Effects of Jasplakinolide on the Kinetics of Actin Polymerization: AN EXPLANATION FOR CERTAIN IN VIVO OBSERVATIONS*". Journal of Biological Chemistry. 275 (7): 5163–5170. doi:10.1074/jbc.275.7.5163. ISSN 0021-9258. PMID 10671562.

[3] "Jasplakinolide | Actin Polymerization Inducer | MedChemExpress". MedchemExpress.com. Retrieved 2025-08-02.

[4] Bubb, M. R.; Senderowicz, A. M.; Sausville, E. A.; Duncan, K. L.; Korn, E. D. (1994-05-27). "Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin". Journal of Biological Chemistry. 269 (21): 14869–14871. doi:10.1016/S0021-9258(17)36545-6. ISSN 0021-9258. PMID 8195116.

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