Programming Peptide Liquid Crystal Media to Acquire Independent Sets of Residual Dipolar Couplings and Enantiodiscrimination in Multiple Solvent Systems

• Published in: Analytical chemistry (Washington) 2023-12, Vol.95 (48), p.17759-17765
• Main Authors: Qin, Si-Yong, He, Jin-Hao, Zhao, You, Yang, Yan-Ling, Zhang, Ai-Qing, Lei, Xinxiang
• Format: Article
• Language: English
• Subjects: Alignment; Couplings; Hydrophobicity; Liquid crystals; Media; Organic compounds; Peptides; Solvents
• ISSN: 0003-2700; 1520-6882
• DOI: 10.1021/acs.analchem.3c03777

Multiple independent sets of residual dipolar couplings (RDCs) acquired by relying on different alignment media show the great potential for de novo structure determination of organic compounds. However, this methodology is severely compromised by the limited availability of multialignment media. In this work, an engineering strategy was developed to program the oligopeptide amphiphiles (OPAs) to create different peptide liquid crystal (LC) media for the acquisition of independent sets of RDCs. With no need for de novo design on peptide sequences, the molecular alignment can be simply modulated by varying the length of the hydrophobic tails within OPAs. Relying on these programmed peptide LC media, five independent sets of RDCs were extracted in a highly efficient and accurate manner. Because of the similar bulk composition of OPAs, this approach offers the significant advantage in circumventing the possible incompatibilities of analytes with one or several different alignment media, therefore avoiding the analysis complication. Notably, these peptide LC media show enantiodifferentiating properties, and the enantiodiscriminating capabilities could also be optimized through the programmed strategy. Furthermore, we show that these media are compatible with different polar solvents, allowing the possible de novo structure elucidation of organic compounds with varied polarities and solubilities.