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Ring Polymers of Tubulin Induced by Binding of Natural Antimitotic Peptides
Author(s) -
Sackett Dan L.
Publication year - 2004
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.200550102
Subject(s) - tubulin , depsipeptide , depolymerization , antimitotic agent , microtubule , cytotoxicity , chemistry , homogeneous , peptide , amino acid , polymer , stereochemistry , ring (chemistry) , in vitro , biophysics , biochemistry , biology , organic chemistry , microbiology and biotechnology , physics , thermodynamics
A number of natural products with potent antimitotic activity are peptides and depsipeptides that bind to tubulin, provoke depolymerization of microtubules, and induce formation of single layer rings of tubulin dimers. These peptides are all hydrophobic and small relative to tubulin (3‐5 amino acid residues), yet induce rings polymers with properties that can differ significantly in size and self‐association. In addition, these compounds exhibit potent cytotoxicity that varies by several hundred fold from one compound to another. Cryptophycin induces unusually homogeneous rings, composed of eight tubulin dimers, that are stable to dilution at least to nanomolar tubulin concentrations.