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The specific interaction between LSD and serotonin-binding protein

J C Shih, J Rho

    Research Communications in Chemical Pathology and Pharmacology
    |April 1, 1977
    PubMed
    Summary
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    This study reveals how lysergic acid (LSD) interacts with serotonin-binding protein (SBP) using advanced spectroscopy. The drug-protein binding causes significant shifts in LSD

    Area of Science:

    • Biochemistry
    • Pharmacology
    • Spectroscopy

    Background:

    • Lysergic acid (LSD) is a psychoactive drug with complex interactions within the biological system.
    • Serotonin-binding protein (SBP) plays a role in regulating serotonin levels.
    • Understanding drug-protein interactions is crucial for pharmacology and toxicology.

    Purpose of the Study:

    • To investigate the chemical interaction between lysergic acid (LSD) and serotonin-binding protein (SBP).
    • To characterize the spectroscopic changes upon LSD binding to SBP.
    • To evaluate the specificity of LSD-SBP interaction compared to other proteins.

    Main Methods:

    • Utilized a three-dimensional spectroscopic technique to record simultaneous activation and fluorescence spectra.
    • Analyzed fluorescence intensity using isointensity contours.

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  • Incubated LSD with SBP and bovine serum albumin (BSA) under controlled conditions.

    • Main Results:

    • Free LSD showed fluorescence maximum at 435 nm and excitation maximum at 330 nm.
    • LSD bound to SBP exhibited a shift in fluorescence maximum to 465 nm and excitation maximum to 375 nm.
    • No significant spectral shift was observed when LSD was incubated with BSA, indicating specific interaction with SBP.

    Conclusions:

    • The observed spectral shifts indicate extensive delocalization of molecular orbital electrons in LSD upon binding to SBP.
    • This delocalization suggests an alteration in the electronic conjugation of the LSD molecule due to protein interaction.
    • The spectroscopic technique is sensitive, requires minimal sample volume, and can differentiate between free and bound drug, providing specific insights into drug-protein interactions.