Ekida T, Nishimura C, Masuda S, Itoh S, Shimada I, Arata Y
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Biochem Biophys Res Commun. 1992 Nov 30;189(1):211-20. doi: 10.1016/0006-291x(92)91546-3.
In order to locate the receptor-binding region of human interleukin-6 (IL-6), twelve peptide fragments were prepared by digestion of IL-6 with lysylendopeptidase. A significant activity of the receptor-binding was observed only for a peptide Ile88-Lys121, although the activity was estimated at 10(4)-fold less than that of intact IL-6. Solution structure of the peptide Ile88-Lys121 was analyzed by using two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The results indicate the presence of alpha-helices in the regions Leu93-Phe106 and Glu110-Ser119. On the basis of the NMR data, we also prepared two peptides. Four-fold less binding activity than that of the peptide Ile88-Lys121 was observed for the peptide Ile88-Arg105, but no activity for the peptide Glu110-Lys121. These results suggest that the helical peptide Ile88-Arg105 composes a part of the receptor-binding region.
为了定位人白细胞介素-6（IL-6）的受体结合区域，用赖氨酰内肽酶消化IL-6制备了12个肽片段。仅对于肽Ile88-Lys121观察到显著的受体结合活性，尽管该活性估计比完整IL-6的活性低10^4倍。通过使用二维核磁共振（NMR）光谱分析肽Ile88-Lys121的溶液结构。结果表明在Leu93-Phe106和Glu110-Ser119区域存在α-螺旋。基于NMR数据，我们还制备了两个肽。对于肽Ile88-Arg105观察到的结合活性比肽Ile88-Lys121低四倍，但对于肽Glu110-Lys121没有活性。这些结果表明螺旋肽Ile88-Arg105构成受体结合区域的一部分。
