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Interaction of novel thiocolchicine analogs with the tubulin isoforms from bovine brain

  1. Author:
    Banerjee, A.
    Kasmala, L. T.
    Hamel, E.
    Sun, L.
    Lee, K. H.

  2. Author Address

    Banerjee A Univ Texas, Hlth Sci Ctr, Dept Biochem San Antonio, TX 78284 USA Univ Texas, Hlth Sci Ctr, Dept Biochem San Antonio, TX 78284 USA NCI, NIH Frederick, MD 21702 USA Univ N Carolina, Nat Prod Lab Chapel Hill, NC 27599 USA
    1. Year: 1999
  2. Journal: Biochemical and Biophysical Research Communications
    1. 254
    2. 2
    3. Pages: 334-337
  4. Type of Article: Article
  1. Abstract:

    The antimitotic alkaloid colchicine binds to tubulin and inhibits microtubule assembly. Recently a new series of colchicine derivatives has been synthesized in which the seven-membered B-ring was Shortened to a six-membered ring. In an effort to study the role of the B-ring substituents in this new series, we have studied the interaction of two compounds of this series, THC 5 and THC 18, with tubulin isoforms from bovine brain. We find that THC 18, which has a side chain with a pi-bonded SP2 conformation, binds differently to the tubulin isoforms, while THC 5 with a slightly different side chain does not. The results indicate that the conformation of the B-ring domain plays a major role in the differential interaction of a colchicine derivative with different tubulin isoforms. The results will be very important in designing potent antitumor derivatives of colchicine. (C) 1999 Academic Press. [References: 23]

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