Journal
MOLECULAR DIVERSITY
Volume 18, Issue 2, Pages 357-373Publisher
SPRINGER
DOI: 10.1007/s11030-014-9507-9
Keywords
Hemiasterlin; Antimitotic peptides; Tubulin; Cytotoxicity; Dynamic resolution
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Funding
- Intramural NIH HHS [Z99 CA999999] Funding Source: Medline
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A representative series of structural analogs of the antimitotic tripeptides hemiasterlins have been designed and synthesized, as potential inhibitors of tubulin polymerization. Relying also on a computational approach, we aimed to explore unknown extensive changes at the C-fragment, by incorporating the conformationally required double bond into five- and six-membered rings. Key steps of the synthetic strategy are a dynamic resolution affording the A-fragment in 97 % ee and the preparation of six new cyclic C fragments, all potentially able to interact with tubulin by means of H bonds. Unexpectedly, biological evaluation of these analogs did not provide evidences neither for cytotoxic effect nor for inhibition of tubulin polymerization.
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