Can the Partial Peptide SIVSF of the β2-Adrenergic Receptor Recognize Chirality of the Epinephrine Neurotransmitter?
Can the Partial Peptide SIVSF of the β2-Adrenergic Receptor Recognize Chirality of the Epinephrine Neurotransmitter?
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β2-肾上腺素受体的部分肽SIVSF能否识别肾上腺素神经递质的手性？
DOI：
10.1021/acs.jpclett.9b00184
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Fujii Masaaki
中科院分区：
文献类型：
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作者：
Tamura Masato;Sekiguchi Tsubasa;Ishiuchi Shun-ichi;Zehnacker-Rentien Anne;Fujii Masaaki
手性在生物分子识别中起着重要的作用，如神经传递。在这里，我们将电喷雾冷离子阱光谱应用于β 2-肾上腺素能受体口袋的部分结合基序SIVSF与L-和D-肾上腺素AdH+的复合物。当L-AdH+被其对映体取代时，SIVSF-AdH+复合物的紫外光谱发生了急剧变化。异构体选择性红外光谱表明，D-AdH+通过其质子化的氨基或单个邻苯二酚OH与SIVSF结合，并诱导SIVSF的非螺旋二级结构。这与具有L-AdH+的螺旋SIVSF复合物形成鲜明对比，其接近于在受体中具有两个儿茶酚OH结合的天然结合结构。这表明短的五肽SIVSF可以区分配体AdH+和受体的手性。这种立体选择性是由涉及手性碳上羟基的额外相互作用引起的。
Chirality plays an essential role in biological molecular recognition, such as neurotransmission. Here, we applied electrospray–cold ion trap spectroscopy to complexes of a partial binding motif SIVSF of a β2-adrenergic receptor pocket with L- and D-epinephrine AdH+. The ultraviolet spectrum of the SIVSF-AdH+complex changed drastically when L-AdH+was replaced by its enantiomer. The isomer-selected infrared spectra revealed that D-AdH+was bound to SIVSF by its protonated amino-group or a single catechol OH and induced nonhelical secondary structures of SIVSF. This is in sharp contrast to the helical SIVSF complex with L-AdH+, which is close to the natural binding structure with two catechol OHs binding in the receptor. This shows that a short pentapeptide SIVSF can distinguish the chirality of the ligand AdH+as well as the receptor. This stereoselectivity is suggested to arise from an additional interaction involving the hydroxyl group on the chiral carbon.