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Chiral Selective Adhesion of Protein Droplets on Calix[4]arene-Enantiomer-Modified Surfaces
ACS Applied Bio Materials ( IF 4.6 ) Pub Date : 2020-01-23 , DOI: 10.1021/acsabm.9b01114
Yuxiao Mei 1, 2 , Jiaxin Quan 1, 2 , Yulin Gu 1 , Yuxia Yang 1 , Jinmei Huang 2 , Kunpeng Sun 1 , Haibing Li 2
Affiliation  

Chiral-specific assembly is involved in many biochemical processes, such as DNA hybridization, protein adhesion, and sugar recognition. However, the signals of chiral interaction are usually very weak, and it is difficult to investigate the enantioselective behaviors. Therefore, it is necessary to construct the functional materials to regulate the selective behaviors of protein droplets via weak chiral interaction, which is also significant for the biological process of protein adhesive behaviors and proteinic drug delivery. Here, S- and R-amino alcohol derivative of calix[4]arene enantiomers (R/S-AC4) were synthesized and modified onto Au-surfaces to fabricate the enantiomer’s materials and investigate the chiral selective adhesion of protein droplets. Through the experiment of fluorescence titration and molecular docking simulation, bovine serum albumin (BSA) showed the stronger interaction with R-amino alcohol-calix[4]arene than S-amino alcohol-calix[4]arene on the molecular level. Notably, the sliding angle showed that the droplet of BSA selectively adhered to the R-amino alcohol-calix[4]arene-modified surface, while it released rapidly from S-amino alcohol-calix[4]arene-modified surface by virtue of chiral selectivity. This result not only provides an easy and convenient model to regulate the selective adhesion and release of protein from chemical view, but also realizes the signal transduction through the weak chiral interaction.

中文翻译:

杯[4]芳烃-对映异构体修饰表面上蛋白液滴的手性选择性粘附

手性特异性组装涉及许多生化过程,例如 DNA 杂交、蛋白质粘附和糖识别。然而,手性相互作用的信号通常非常微弱,很难研究对映选择性行为。因此,有必要构建功能材料,通过弱手性相互作用调节蛋白液滴的选择性行为,这对于蛋白质粘附行为和蛋白质药物递送的生物学过程也具有重要意义。在这里,合成了杯[4]芳烃对映异构体(R/S-AC4)的S-和R-氨基醇衍生物,并在Au表面上进行了修饰,以制备对映异构体材料并研究蛋白质液滴的手性选择性粘附。通过荧光滴定实验和分子对接模拟,牛血清白蛋白(BSA)在分子水平上与R-氨基醇-杯[4]芳烃的相互作用比S-氨基醇-杯[4]芳烃更强。值得注意的是,滑动角表明,BSA液滴选择性地粘附在R-氨基醇-杯[4]芳烃修饰的表面上,同时通过S-氨基醇-杯[4]芳烃修饰的表面迅速释放出来。手性选择性。该结果不仅为从化学角度调控蛋白质选择性粘附和释放提供了一个简单方便的模型,而且通过弱手性相互作用实现了信号转导。滑动角表明,BSA液滴选择性地附着在R-氨基醇-杯[4]芳烃修饰的表面上,同时凭借手性选择性从S-氨基醇-杯[4]芳烃修饰的表面快速释放。 . 该结果不仅为从化学角度调控蛋白质选择性粘附和释放提供了一个简单方便的模型,而且通过弱手性相互作用实现了信号转导。滑动角表明,BSA液滴选择性地附着在R-氨基醇-杯[4]芳烃修饰的表面上,同时凭借手性选择性从S-氨基醇-杯[4]芳烃修饰的表面快速释放。 . 该结果不仅为从化学角度调控蛋白质选择性粘附和释放提供了一个简单方便的模型,而且通过弱手性相互作用实现了信号转导。
更新日期:2020-01-23
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