Chemical and Pharmaceutical Bulletin
Online ISSN : 1347-5223
Print ISSN : 0009-2363
ISSN-L : 0009-2363
Notes
Two New Ring-Contracted Congeners of Rhizopodin Illustrate Significance of the Ring Moiety of Macrolide Toxins on the Actin Disassembly-Mediated Cytotoxicity
Naoya OkuAyaka MatsumotoTakayuki MatsunagaYuhki AsanoHiroaki KasaiShouhei MatobaYasuhiro Igarashi
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2014 Volume 62 Issue 3 Pages 294-300

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Abstract

Two new cytotoxic dilactones, bisisorhizopodin (1) and isorhizopodin (2), together with known divalent actin depolymerizer rhizopodin (3), were isolated from the culture broth of a myxobacterium Myxococcus stipitatus. Spectroscopic analyses established that 1 and 2 are doubly and singly acyl-migrated isomers of 3, respectively, and comparison of their cytotoxicity revealed gradual decrease in the activity as the size of the ring contracted. Because the side chains of macrolide toxins uniformly block the contact between the actin protomers, the present result demonstrates substantial contribution of structurally diverse rings to the affinity of macrolide toxins for its target protein.

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© 2014 The Pharmaceutical Society of Japan
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