Oba Makoto, Ito Chika, Tanaka Masakazu
Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
Bioorg Med Chem Lett. 2018 Mar 1;28(5):875-877. doi: 10.1016/j.bmcl.2018.02.002. Epub 2018 Feb 9.
A five-membered ring amino acid (Acc), the peptides of which exhibit a preference for helical secondary structures, was introduced into peptides for the purpose of designing coiled coil peptides with high binding affinities. We prepared five types of peptides containing Acc with different numbers or at different positions. The incorporation of Acc into peptides enhanced their α-helicities; however, in contrast to our expectations, it did not result in stable coiled coil formation. The structures of side chains in hydrophobic amino acids, not α-helicities appeared to be important for stable hydrophobic interactions between peptides. Although we were unable to develop coiled coil peptides with high binding affinities, the present results will be useful for designing novel coiled coil peptides.
一种五元环氨基酸（Acc），其肽段对螺旋二级结构具有偏好性，为了设计具有高结合亲和力的卷曲螺旋肽而被引入到肽中。我们制备了五种含有不同数量或处于不同位置的Acc的肽。将Acc掺入肽中增强了它们的α-螺旋度；然而，与我们的预期相反，这并未导致稳定的卷曲螺旋形成。疏水氨基酸侧链的结构，而非α-螺旋度，似乎对肽之间稳定的疏水相互作用很重要。尽管我们未能开发出具有高结合亲和力的卷曲螺旋肽，但目前的结果将有助于设计新型卷曲螺旋肽。
