Novel instrumentation and biomedical applications of very near-infrared fluorescence

Marc Brown, T. E. Edmonds, J. N. Miller, D. P. Riley, N. J. Seare

    Research output: Contribution to journalArticlepeer-review

    Abstract

    A high wavelength fluorescent probe, Nile Red, was added to four proteins, viz., bovine albumin, alpha1-acid glycoprotein, beta-lactoglobulin and ovomucoid. Nile Red showed an enhancement in fluorescence and a shift in emission wavelength, suggesting it was bonding hydrophobically to these proteins. Drug displacement of Nile Red from alpha1-acid glycoprotein was achieved with both D,L-propranolol and flufenamic acid, showing that the binding site is less electrostatic and more hydrophobic in nature. In order to monitor these interactions, a simple spectrofluorimeter was constructed from solid-state components; the sensitivity of this instrument compared well with that of standard laboratory spectrofluorimeters.

    Original languageEnglish
    Pages (from-to)407-410
    Number of pages4
    JournalAnalyst
    Volume118
    Issue number4
    Publication statusPublished - Apr 1993

    Keywords

    • VERY NEAR INFRARED FLUORESCENCE
    • SOLID-STATE SPECTROFLUOROMETRY
    • BIOMEDICAL APPLICATIONS
    • NILE RED
    • ALPHA-1-ACID GLYCOPROTEIN
    • HUMAN-SERUM
    • BINDING
    • PROBE
    • SURFACES
    • ALBUMIN
    • DRUGS

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