Conformational selectivity in molecular recognition: the influence of artificial receptors on the cis-trans isomerization of acylprolines

• Published in: Journal of the American Chemical Society Vol. 113; no. 14; pp. 5466 - 5467
• Main Authors: Vicent, Cristina, Hirst, Simon C, Garcia-Tellado, Fernando, Hamilton, Andrew D
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01.07.1991
• Subjects: Atomic and molecular physics; Exact sciences and technology; General molecular conformation and symmetry; stereochemistry; Molecular properties and interactions with photons; Physics; Properties of molecules and molecular ions; Isomerization; NMR spectrometry; Selectivity; Experimental study; NMR spectrum; Organic compounds; Conformation; Macrocycle
• ISSN: 0002-7863; 1520-5126
• DOI: 10.1021/ja00014a055

The cis-trans isomerization of acylprolyl groups is a kinetically significant step in protein folding and, as such, has been the subject of intense scrutiny. This interest has increased with the recent identification of a family of enzymes that catalyze this interconversion and the important role that two of their number, cyclophilin and FK506 binding protein, play in immunosupression. The peptidyl prolyl isomerases (PPIases) have been investigated by spectroscopic, synthetic, and kinetic methods, and a catalytic mechanism involving amide-bond distortion has been proposed. We report herein that different synthetic receptors can discriminate between the two rotamers and so influence the acylproline s-cis-s-trans equilibrium.