Can the Partial Peptide SIVSF of β 2 -Adrenergic Receptor Recognize Chirality of Epinephrine Neurotransmitter?

Masato Tamura , Tsubasa Sekiguchi , Shun-Ichi Ishiuchi (1) , Anne Zehnacker-Rentien (2, 3) , Masaaki Fujii (1)

1 Chemical Resources Laboratory, Tokyo Institute of Technology
2 ISMO - Institut des Sciences Moléculaires d'Orsay
3 SYSIPHE

(148 words) Chirality plays an essential role in biological molecular recognition such as neurotransmission. Here, we apply electrospray (ESI)-cold ion trap spectroscopy to complexes of a partial binding motif SIVSF of 2-adrenergic receptor pocket with Land 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 intrinsic 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.

Domaines: Chimie

Masato Tamura, Tsubasa Sekiguchi, Shun-Ichi Ishiuchi, Anne Zehnacker-Rentien, Masaaki Fujii. Can the Partial Peptide SIVSF of β 2 -Adrenergic Receptor Recognize Chirality of Epinephrine Neurotransmitter?. Journal of Physical Chemistry Letters, 2019, ⟨10.1021/acs.jpclett.9b00184⟩. ⟨hal-02070253⟩