Extremely strong tubular stacking of aromatic oligoamide macrocycles† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c4sc02380c Click here for additional data file.

نویسندگان

  • Mark A. Kline
  • Xiaoxi Wei
  • Ian J. Horner
  • Rui Liu
  • Shuang Chen
  • Si Chen
  • Ka Yi Yung
  • Kazuhiro Yamato
  • Zhonghou Cai
  • Frank V. Bright
  • Xiao Cheng Zeng
  • Bing Gong
چکیده

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منابع مشابه

Large ring-forming alkylations provide facile access to composite macrocycles† †Electronic supplementary information (ESI) available: Fig. S1–S4, list of macrocycles prepared, experimental procedures, and spectroscopic data. CCDC 1023942. For ESI and crystallographic data in CIF or other electronic format see DOI: 10.1039/c4sc03848g Click here for additional data file. Click here for additional data file.

Macrocyclic compounds have potential to enable drug discovery for protein targets with extended, solventexposed binding sites. Crystallographic structures of peptides bound at such sites show strong surface complementarity and frequent aromatic side-chain contacts. In an effort to capture these features in stabilized small molecules, we describe a method to convert linear peptides into constrai...

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Orthogonal functionalisation of α-helix mimetics† †Electronic supplementary information (ESI) available: Additional binding data and fluorescence characterisation. Experimental procedures and characterisation of all new compounds. See DOI: 10.1039/c4ob00915k Click here for additional data file.

α-Helix mediated protein-protein interactions are of major therapeutic importance. As such, the design of inhibitors of this class of interaction is of significant interest. We present methodology to modify N-alkylated aromatic oligoamide α-helix mimetics using 'click' chemistry. The effect is shown to modulate the binding properties of a series of selective p53/hDM2 inhibitors.

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عنوان ژورنال:

دوره 6  شماره 

صفحات  -

تاریخ انتشار 2015