Rist B, Wieland H A, Willim K D, Beck-Sickinger A G
Department of Pharmacy, ETH Zürich, Switzerland.
J Pept Sci. 1995 Sep-Oct;1(5):341-8. doi: 10.1002/psc.310010509.
Four sets of centrally truncated analogues of neuropeptide Y have been synthesized. In each series the N-terminal part was constant, while the C-terminal segment was systematically varied in length. The C- and N-terminal parts were linked by 6-aminohexanoic acid. The affinity to the Y1 receptor was investigated on human neuroblastoma cells SK-N-MC. Significant differences were found between the series of peptides as well as within each set. Remarkably, the affinity did not solely depend on the length of the segment, and with increasing numbers of residues the IC50 values were not always decreased. With a given N-terminal segment, only one optimal length of the C-terminal segment was found, which suggests that it is not the amino acids themselves but their 3D arrangement and orientation that is important for high receptor affinity.
已合成了四组神经肽Y的中央截短类似物。在每个系列中，N端部分是恒定的，而C端片段的长度则系统地变化。C端和N端部分通过6-氨基己酸连接。在人神经母细胞瘤细胞SK-N-MC上研究了对Y1受体的亲和力。在肽系列之间以及每组内都发现了显著差异。值得注意的是，亲和力并不完全取决于片段的长度，并且随着残基数量的增加，IC50值并不总是降低。对于给定的N端片段，仅发现C端片段的一个最佳长度，这表明对于高受体亲和力而言，重要的不是氨基酸本身，而是它们的三维排列和取向。
