83830-88-0Relevant academic research and scientific papers
Stabilizing amyloid-β peptide by the N-terminus capture is capable of preventing and eliminating amyloid-β oligomers
Wen, Gesi,Chen, Daoyuan,Qin, Wenjing,Zhou, Binhua,Wang, Youqiao,Liu, Ziyi,Du, Jun,Zhou, Qiang,Quan, Junmin,Bu, Xianzhang
supporting information, p. 7673 - 7676 (2017/07/12)
Elimination of amyloid-β (Aβ) oligomers remains challenging. We describe here a novel strategy to prevent and eliminate the Aβ oligomers from either the early aggregation or the fibril dissolution pathway by targeting the flexible N-terminus, but not the widely investigated hydrophobic segment, with a rationally designed cyclopeptide.
Solvent-free thermocyclization of the unactivated linear gramicidin S precursor and analogues
An, Lin-Kun,Li, Run-Lin,Zuo, Ying-Lin,Gu, Lian-Quan
supporting information; experimental part, p. 34 - 37 (2011/03/22)
A convenient thermocyclization of the linear gramicidin S precursor and its analogues is demonstrated. With the preorganized β-sheet conformation, the unactivated linear precursors can cyclize into the corresponding head-to-tail cyclic products in high yield after being heated under solvent-free conditions.
