Jiangsu Key Laboratory of Advanced Catalytic Materials and Technology , Changzhou University , Changzhou 213164 , China.
Anal Chem. 2019 Sep 17;91(18):11864-11871. doi: 10.1021/acs.analchem.9b02605. Epub 2019 Aug 23.
Stereospecific molecular recognition with simple and easily available proteins is of significant importance in life science and biomaterial science. Herein, we report on a chiral sensing platform, graphene quantum dots (GQDs)-functionalized bovine serum albumin (BSA), for chiral recognition of tryptophan (Trp) isomers. Amidation reaction between BSA and GQDs was directly responsible for the introduction of GQDs to BSA, resulting in significant changes in the spatial configuration of BSA and the exposure of more chiral sites at the protein surface. The BSA-GQDs-based chiral sensor exhibited good biomolecular homochirality in the recognition of Trp isomers, and the higher affinity of BSA-GQDs toward l-Trp than its isomer, d-Trp, was also revealed by density functional theory (DFT) considering the possible hydrogen bonds between the Trp isomers and the solvent-accessible residues of BSA.
手性分子识别与简单易得的蛋白质在生命科学和生物材料科学中具有重要意义。在此，我们报告了一种手性传感平台，即石墨烯量子点（GQDs）功能化牛血清白蛋白（BSA），用于对色氨酸（Trp）异构体的手性识别。BSA 与 GQDs 之间的酰胺化反应直接导致 GQDs 引入到 BSA 中，从而导致 BSA 的空间构象发生显著变化，并在蛋白质表面暴露出更多的手性位点。基于 BSA-GQDs 的手性传感器在手性识别色氨酸异构体方面表现出良好的生物分子同手性，并且密度泛函理论（DFT）也表明 BSA-GQDs 对 l-Trp 的亲和力高于其异构体 d-Trp，这是考虑到色氨酸异构体与 BSA 溶剂可及残基之间可能的氢键的结果。
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