Premium
The tertiary amine local anesthetic dibucaine binds to the membrane skeletal protein spectrin
Author(s) -
Mondal Mousumi,
Chakrabarti Abhijit
Publication year - 2002
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/s0014-5793(02)03721-3
Subject(s) - dibucaine , chemistry , dissociation constant , tetracaine , tertiary amine , biophysics , spectrin , photochemistry , biochemistry , organic chemistry , lidocaine , medicine , receptor , anesthesia , biology , cytoskeleton , cell
The quinoline‐based tertiary amine dibucaine has been shown to bind the membrane skeletal protein spectrin with a dissociation constant of 3.5×10 −5 M at 25°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.