Journal
ORGANIC & BIOMOLECULAR CHEMISTRY
Volume 20, Issue 14, Pages 2922-2938Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2ob00118g
Keywords
-
Categories
Funding
- JSPS KAKENHI [26242073, 18H04606, 20H04764, 20H02865, 18K14343, 20K05722]
- Uehara Memorial Foundation
- Naito Foundation
- Grants-in-Aid for Scientific Research [20H02865, 20K05722, 20H04764, 18K14343, 18H04606] Funding Source: KAKEN
Ask authors/readers for more resources
In this study, an aplyronine A-swinholide A hybrid was designed, synthesized, and evaluated for its biological activity. The methoxy group in the N,N,O-trimethylserine ester was found to be important for the compound's activity, and the side chain analog of swinholide A exhibited weaker actin-depolymerizing activity compared to that of aplyronine A.
An aplyronine A-swinholide A hybrid, consisting of the macrolactone part of aplyronine A and the side chain part of swinholide A, was designed, synthesized, and biologically evaluated. This hybrid induced protein-protein interactions between two major cytoskeletal proteins actin and tubulin in the same manner as aplyronine A, and exhibited potent cytotoxicity and actin-depolymerizing activity. The importance of the methoxy group in the N,N,O-trimethylserine ester was clarified by the structure-activity relationship studies of the amino acid moiety by using the hybrid analogs. Furthermore, the comparison of the actin-depolymerizing activities between the side chain analogs of aplyronine A and swinholide A showed that the side chain analog of swinholide A had much weaker actin-depolymerizing activity than that of aplyronine A.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available