Abstract
The review focuses on the unique spectral features of pyrene that can be utilized to investigate protein structure and conformation. Pyrene is a fluorescent probe that can be attached covalently to protein side chains, such as sulfhydryl groups. The spectral features of pyrene are exquisitely sensitive to the microenvironment of the probe: it exhibits an ensemble of monomer fluorescence emission peaks that report on the polarity of the probe microenvironment, and an additional band at longer wavelengths, the appearance of which reflects the presence of another pyrene molecule in spatial proximity (~10 Å). Its high extinction coefficient allows us to study labeled proteins in solution at physiologically relevant concentrations. The environmentally- and spatially-sensitive features of pyrene allow monitoring protein conformation, conformational changes, protein folding and unfolding, protein-protein, protein-lipid and protein-membrane interactions.
Highlights
Biochemists and biophysicists have an arsenal of fluorescent probes at their disposal to understand the molecular organization of biological molecules
The exchangeable class of apolipoproteins is used to illustrate the application of pyrene as a fluorescent probe to study protein conformation, conformational changes and dynamics
Pyrene excimer fluorescence has been employed to monitor protein unfolding, as demonstrated with human carbonic anhydrase II (HCAII), an enzyme containing a zinc ion coordinated to three histidines in its active site [118]
Summary
Biochemists and biophysicists have an arsenal of fluorescent probes at their disposal to understand the molecular organization of biological molecules. This review describes the use of pyrene and its Molecules 2011, 16 derivatives as a probe to study biomolecules. Pyrene is one of the oldest probes to be employed to study a wide range of biomolecules: Lipids, proteins and nucleic acids. The review will focus only on the use of pyrene to monitor conformation and conformational changes in proteins in aqueous solutions. The exchangeable class of apolipoproteins is used to illustrate the application of pyrene as a fluorescent probe to study protein conformation, conformational changes and dynamics. Discussion of pyrene as a probe to study lipids and nucleic acids in membrane biophysics, cell biology and cellular biochemistry is beyond the scope of this review; the reader is referred to comprehensive reviews on these topics [1,2,3,4,5,6]
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