Department of Chemistry, National Tsing Hua University, Hsinchu 30013, Taiwan.
Department of Chemistry, National Tsing Hua University, Hsinchu 30013, Taiwan; Frontier Research Center on Fundamental and Applied Sciences of Matters, National Tsing Hua University, Hsinchu 30013, Taiwan.
Bioorg Chem. 2022 Feb;119:105491. doi: 10.1016/j.bioorg.2021.105491. Epub 2021 Nov 15.
The unique interaction between fluorine atoms has been exploited to alter protein structures and to develop synthetic and analytical applications. To expand such fluorous interaction for novel applications, polyproline peptides represent an excellent molecular nanoscaffold for controlling the presentation of perfluoroalkyl groups on their unique secondary structure. We develop approaches to synthesis fluorinated peptides to systematically investigate how the number, location and types of the fluorous groups on polyproline affect the conformation by monitoring the transition between the two major polyproline structures PPI and PPII. This work provides valuable information on how fluorous interaction affects the peptide structure and also benefits the design of functional fluorous molecules.
氟原子之间的独特相互作用已被利用来改变蛋白质结构，并开发出合成和分析应用。为了将这种氟相互作用扩展到新的应用，多聚脯氨酸肽代表了一种控制全氟烷基在其独特二级结构上呈现的优秀分子纳米支架。我们开发了合成氟化肽的方法，通过监测两种主要的多聚脯氨酸结构 PPI 和 PPII 之间的转变，系统地研究了多聚脯氨酸上氟基团的数量、位置和类型如何影响构象。这项工作提供了有关氟相互作用如何影响肽结构的有价值信息，也有利于功能氟分子的设计。
