Mimics of peptide turn backbone and side-chain geometry by a general approach for modifying azabicyclo[5.3.0]alkanone amino acids.
Mimics of peptide turn backbone and side-chain geometry by a general approach for modifying azabicyclo[5.3.0]alkanone amino acids.
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通过修饰氮杂双环[5.3.0]烷酮氨基酸的通用方法模拟肽的主链和侧链几何形状。
DOI：
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发表时间：
2011
影响因子：
3.6
通讯作者：
W. Lubell
中科院分区：
文献类型：
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作者：
Tanya A. Godina;W. Lubell
具有受限骨架和侧链几何构型的肽模拟物是研究生物活性候选物构效关系的重要工具。已经开发了一种用于产生具有侧链多样性的β-转角模拟物的通用方法，其特征在于碘化物前体的非对映选择性S（N）1置换。特别地，6-碘-吡咯并氮杂环庚三烯-2-酮氨基酯10在与各种醇、苯酚、硝酸盐和叠氮化物亲核试剂的反应中充当共同的前体，以提供一系列受约束的肽模拟物。
Peptide mimics with constrained backbone and side-chain geometry are important tools for studying structure activity relationships of biologically active candidates. A general method for creating β-turn mimics possessing side-chain diversity has been developed featuring diastereoselective S(N)1 displacements of an iodide precursor. In particular, 6-iodo-pyrroloazepin-2-one amino ester 10 has served as a common precursor in reactions with a variety of alcohol, phenol, nitrate, and azide nucleophiles to provide an array of constrained peptide mimics.
影响因子：
7.3
作者：
Zhang B;Nikolovska-Coleska Z;Zhang Y;Bai L;Qiu S;Yang CY;Sun H;Wang S;Wu Y
通讯作者：
Wu Y