Dissociation of tubulin assembly‐inhibiting and aggregation‐promoting activities by a vinblastine derivative

FEBS Letters

Rai, Sadananda S.¹  Wolff, J.¹ 

[1] Laboratory of Biochemical Pharmacology, NIDDK, National Institutes of Health, Bethesda, MD 20892, USA

关键词: Vinblastine;    Vinblastine-4′-anthranilate;    Tubulin assembly inhibition;    Spiral aggregate;    AntVin;    vinblastine-4′-anthranilate;    MES;    2-(N-morpholino) ethanesulfonic acid;    EGTA;    ethyleneglycol-bis-(β-aminoethyl ether) N;    N′-tetraacetic acid;    DMSO;    dimethyl sulfoxide;   

DOI  :  10.1016/S0014-5793(97)01211-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A fluorescent vinblastine analogue, vinblastine-4′-anthranilate (Antvin), that binds to the vinca site on tubulin, inhibits tubulin assembly but does not lead to spiral or other large aggregate formation at concentrations up to 1.6 mM. As judged by turbidity, 90° light scattering and fluorescence anisotropy, little aggregation could be detected. This is in marked contrast to vinblastine and suggests that inhibition of assembly and aggregate formation can be dissociated from each other by suitable substitution in vinblastine.

【 授权许可】

Unknown