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Importance of hydrogen‐bonding sites in the chiral recognition mechanism between racemic D 3 terbium(III) complexes and amino acids
Author(s) -
Moussa Ahmed,
Pham Christine,
Bommireddy Shruthi,
Muller Gilles
Publication year - 2009
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20628
Subject(s) - chemistry , hydrogen bond , chirality (physics) , amino acid , stereochemistry , terbium , luminescence , crystallography , molecule , organic chemistry , biochemistry , ion , chiral symmetry breaking , physics , optoelectronics , quantum mechanics , nambu–jona lasinio model , quark
The perturbation of the racemic equilibrium of luminescent D 3 terbium(III) complexes with chelidamic acid (CDA), a hydroxylated derivative of 2,6‐pyridine‐dicarboxylic acid (DPA), by added chiral biomolecules such as L ‐amino acids has been studied using circularly polarized luminescence and 13 C NMR spectroscopy. It is shown in this work that the chiral‐induced equilibrium shift of [Tb(CDA) 3 ] 6− by L ‐amino acids (i.e. L ‐proline or L ‐arginine) was largely influenced by the hydrogen‐bonding networks formed between the ligand interface of racemic [Tb(CDA) 3 ] 6− and these added chiral agents. The capping of potential hydrogen‐bonding sites by acetylation in L ‐proline led to a ∼100‐fold drop in the induced optical activity of the [Tb(CDA) 3 ] 6− : N ‐acetyl‐ L ‐proline system. This result suggested that the hydrogen‐bonding networks serve as the basis for further noncovalent discriminatory interactions between racemic [Tb(CDA) 3 ] 6− and added L ‐amino acids. Chirality, 2009. © 2008 Wiley‐Liss, Inc.