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The importance of the phenyl‐tropolone ‘ aS ’ configuration in colchicine's binding to tubulin
Author(s) -
Yeh Herman J.C.,
Chrzanowska Maria,
Brossi Arnold
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80802-0
Subject(s) - tropolone , colchicine , tubulin , moiety , stereochemistry , chemistry , enantiomer , microtubule , diene , biology , organic chemistry , microbiology and biotechnology , genetics , natural rubber
Measuring ellipticities of (±)‐colchicine and (±)‐deacetamidocolchicine in the presence of tubulin afforded net positive CD bands with maxima at 340 nm resulting from reduction of the negative ellipticities upon binding of (−) enantiomers to the protein. Results of optical studies together with earlier NMR conformational analysis of these molecules substantiate the hypothesis that colchicinoids bind to tubulin with the phenyl‐tropolone moiety in the ‘ aS ’ configuration. Natural colchicine which binds to tubulin, therefore, should be referred to as (−)‐( aS , 7 S )‐colchicine.