Barden J A, Cuthbertson R M, Potter E K, Selbie L A, Tseng A
Department of Anatomy and Histology, University of Sydney, NSW, Australia.
Biochim Biophys Acta. 1994 Jun 12;1206(2):191-6. doi: 10.1016/0167-4838(94)90207-0.
Neuropeptide Y analog N-acetyl[Leu-28,Leu-31]NPY(24-36)-amide binds specifically to prejunctional or Y2 receptors acting to inhibit neurotransmitter release. The structure of this biologically active mutant was studied by two-dimensional proton nuclear magnetic resonance spectroscopy. Assignments of all backbone and side chain hydrogens were made by using totally correlated spectroscopy (TOCSY) experiments providing through-bond 1H-1H connectivities, and nuclear Overhauser effect spectroscopy (NOESY), which provided through-space and sequential backbone connectivities. Structure analysis of the peptide was performed using distance geometry and dynamic simulated annealing revealing the presence of a helical structure exhibiting an amphiphilic character and slight constriction in the segment 24-29.
神经肽Y类似物N-乙酰基[亮氨酸-28，亮氨酸-31]神经肽Y(24 - 36)-酰胺特异性结合于作用于抑制神经递质释放的突触前或Y2受体。通过二维质子核磁共振光谱研究了这种生物活性突变体的结构。利用提供键间1H-1H连接性的全相关光谱(TOCSY)实验以及提供空间和序列主链连接性的核Overhauser效应光谱(NOESY)对所有主链和侧链氢进行了归属。使用距离几何和动态模拟退火对该肽进行结构分析，揭示了存在一种具有两亲性特征且在24 - 29片段有轻微收缩的螺旋结构。
