68705-66-8
Chemical Structure
Kolaflavanone
- CAS No.: 68705-66-8
- Formula:C31H24O12
- Molecular Weight:588.52
IUPAC Name: (2S,2'R,3R,3'R)-3',5,5',7,7'-pentahydroxy-2'-(3-hydroxy-4-methoxyphenyl)-2-(4-hydroxyphenyl)-[3,8'-bichromane]-4,4'-dione
InChIKey: GJWXCPDVDRIBKP-CNTBMXMRSA-N
SMILES: O=C1[C@@H]([C@H](OC2=CC(O)=CC(O)=C12)C3=CC=C(C=C3)O)C4=C5C(C([C@@H]([C@H](O5)C6=CC=C(C(O)=C6)OC)O)=O)=C(C=C4O)O
Biological Activity: Kolaflavanone is an biflavonoid allosteric inhibitor of Eg5. Kolaflavanone inhibits the ATPase and tyrosinase activities of Eg5 under both basal and microtubule-activated conditions, suppresses microtubule sliding activity, binds to the L5/α2/α3 allosteric pocket of Eg5, induces conformational changes of Eg5 and microtubule dissociation, interacts with aldehyde dehydrogenase, inhibits the ATPase activity of kinesin-1, and binds to HSA via pH-dependent forces. Kolaflavanone exhibits antihepatotoxic activity and can be used in studies related to Phalloidin (HY-P0028)-induced liver injury[1][2][3].
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Kolaflavanone | Kolaflavanone is an biflavonoid allosteric inhibitor of Eg5. Kolaflavanone inhibits the ATPase and tyrosinase activities of Eg5 under both basal and microtubule-activated conditions, suppresses microtubule sliding activity, binds to the L5/α2/α3 allosteric pocket of Eg5, induces conformational changes of Eg5 and microtubule dissociation, interacts with aldehyde dehydrogenase, inhibits the ATPase activity of kinesin-1, and binds to HSA via pH-dependent forces. Kolaflavanone exhibits antihepatotoxic activity and can be used in studies related to Phalloidin (HY-P0028)-induced liver injury. | |||||||||||||||||||||
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References
- [1]. Alrazi IMD, et al. Kolaflavanone, a biflavonoid derived from medicinal plant Garcinia, is an inhibitor of mitotic kinesin Eg5. Journal of biochemistry. 2021 Dec 28;170(5):611-622. [Content Brief]
- [2]. Iwu MM. Antihepatoxic constituents of Garcinia kola seeds. Experientia. 1985 May 15;41(5):699-700. [Content Brief]
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[3]. Kolawole AO, et al. Kolaflavanone of kolaviron selectively binds to subdomain 1B of human serum albumin: spectroscopic and molecular docking evidences. Computational Toxicology. 2020;13:100118.
