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Can the Partial Peptide SIVSF of β 2 -Adrenergic Receptor Recognize Chirality of Epinephrine Neurotransmitter?
Journal of Physical Chemistry Letters 2019 March 7
Chirality plays an essential role in biological molecular recognition such as neurotransmission. Here, we apply electrospray - cold ion trap spectroscopy to complexes of a partial binding motif SIVSF of β2 -adrenergic receptor pocket with L- and D-epinephrine AdH+ . The UV spectrum of the SIVSF-AdH+ complex is changed drastically when L-AdH+ is replaced by its enantiomer. The isomer-selected IR spectra reveal that D-AdH+ is bound to SIVSF by its protonated amino-group or a single catechol OH, and induces non-helical secondary structures of SIVSF. It is sharp contrast to the helical SIVSF complex with L-AdH+ , which is close to the natural binding structure with two catechol OH binding in the receptor. It shows that a short pentapeptide SIVSF can distinguish chirality of the ligand AdH+ as well as the receptor. This stereoselectivity is suggested to arise from the additional interaction involving the hydroxyl group on the chiral carbon.
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