Send to

Choose Destination
See comment in PubMed Commons below
Chem Pharm Bull (Tokyo). 2014;62(3):294-300.

Two new ring-contracted congeners of rhizopodin illustrate significance of the ring moiety of macrolide toxins on the actin disassembly-mediated cytotoxicity.

Author information

Biotechnology Research Center and Department of Biotechnology, Toyama Prefectural University.


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.

[Indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for J-STAGE, Japan Science and Technology Information Aggregator, Electronic
    Loading ...
    Support Center