The tertiary amine local anesthetic dibucaine binds to the membrane skeletal protein spectrin.

FEBS Lett

Chemical Sciences Division, Saha Institute of Nuclear Physics, 1/AF Bidhannagar, 700064, Calcutta, India.

Published: December 2002

The quinoline-based tertiary amine dibucaine has been shown to bind the membrane skeletal protein spectrin with a dissociation constant of 3.5x10(-5) M at 25 degrees C. Such binding is detected by monitoring the quenching of the tryptophan fluorescence intensity with increasing concentrations of dibucaine only and not with the benzene-based local anesthetics procaine, tetracaine and lidocaine. Binding of dibucaine also indicated changes in the tertiary structure of spectrin indicated by a circular dichroism spectrum in the near-UV region due to absorption of the aromatic side chains. The thermodynamic parameters associated with the binding indicated the interaction of dibucaine and spectrin to be enthalpy-driven and insensitive to an increase in the ionic strength of the buffer.

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http://dx.doi.org/10.1016/s0014-5793(02)03721-3DOI Listing

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