Phosphorylated peptides are instrumental in studying protein phosphorylation events. In the present study, Raman optical activity (ROA) is employed to elucidate the structure of a dipeptide, L-alanyl-L-glutamine (L-Ala-L-Gln) and its two differently alkylated N-phosphorylated derivatives. Theoretical simulations were conducted to aid the interpretation of peptide conformation variations upon phosphorylation, and of the measured Raman and ROA spectra. Induced circularly polarized luminescence (CPL) was also recorded in solution, in the presence of a simple europium aqua ion. As the spectra are peptide specific, this type of stereochemical analysis is expected to aid identification of the phosphorylation sites also in other peptides and possibly proteins.

Institute of Drug Discovery Technology Ningbo University 315 211 Ningbo Zhejiang China; Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences Ningbo University Ningbo 315 211 China

Institute of Drug Discovery Technology Ningbo University 315 211 Ningbo Zhejiang China; Qian Xuesen Collaborative Research Center of Astrochemistry and Space Life Sciences Ningbo University Ningbo 315 211 China; Department of Chemical Biology College of Chemistry and Chemical Engineering Xiamen University Xiamen 361 005 China

Institute of Organic Chemistry and Biochemistry Czech Academy of Sciences Flemingovo náměstí 2 166 10 Prague 6 Czech Republic

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