Cover Feature: Heat Shock Proteins Revisited: Using a Mutasynthetically Generated Reblastatin Library to Compare the Inhibition of Human and Leishmania Hsp90s (ChemBioChem 6/2018),ChemBioChem

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Cover Feature: Heat Shock Proteins Revisited: Using a Mutasynthetically Generated Reblastatin Library to Compare the Inhibition of Human and Leishmania Hsp90s (ChemBioChem 6/2018)
ChemBioChem ( IF 2.6 ) Pub Date : 2018-03-05 , DOI: 10.1002/cbic.201800104
Sona Mohammadi-Ostad-Kalayeh ₁ , Frank Stahl ₂ , Thomas Scheper ₂ , Klaus Kock ₃ , Christian Herrmann ₃ , Fernanda Aparecida Heleno Batista ₄ , Júlio César Borges ₄ , Florenz Sasse ₅ , Simone Eichner ₆ , Jekaterina Ongouta ₆ , Carsten Zeilinger ₁ , Andreas Kirschning ₆

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The cover feature picture shows new reblastatin derivatives obtained by a chemo‐biosemisynthetic approach with the corresponding aminobenzoic acid derivatives as starting building blocks. The fluoro and amino derivatives exerted high inhibitory activity on human and leishmania Hsp90, whereas the presence of an alkynyl substituent leads to selective activity towards Hsp90 from leishmania. The inhibitory activity was unraveled by using a novel protein microarray system with purified Hsp90 proteins and was further confirmed by cell‐based assays and ITC measurements. More information can be found in the full paper by C. Zeilinger, A. Kirschning et al. on page 562 in Issue 6, 2018 (DOI: 10.1002/cbic.201700616).

中文翻译：

封面文章：重温热激蛋白：使用多合成生成的Relastatin文库来比较人类和利什曼原虫Hsp90s的抑制作用（ChemBioChem 6/2018）

封面特征图片显示了通过化学二糖杂合成法获得的新的视网膜抑素衍生物，并以相应的氨基苯甲酸衍生物作为起始结构单元。氟和氨基衍生物对人和利什曼原虫Hsp90具有很高的抑制活性，而炔基取代基的存在导致对利什曼原虫对Hsp90的选择性活性。通过使用具有纯化的Hsp90蛋白质的新型蛋白质微阵列系统，可以揭示抑制活性，并通过基于细胞的测定和ITC测量进一步证实了抑制活性。在C. Zeilinger，A. Kirschning等人的全文中可以找到更多信息。就在第6期，2018页562（：10.1002 / cbic.201700616 DOI）。

更新日期：2018-03-05

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