β Scribed by Tetsuo Shiba; Hiroshi Uratani; Ichiro Kubota; Yoshihiko Sumi
No coin nor oath required. For personal study only.
A conformation of a diketopiperazine, cyclo(LβleucylβLβtryptophyl), was determined by nmr and xβray analysis. The receptor for this bitter diketopiperazine neither recognizes chirality nor requires a strict conformation of the substrate. A good correlation was found between the bitterness of diketopiperazine and its hydrophobicity. Experiments using liposome as a model of the receptor membrane suggested that a lecithinβlike lipid is a candidate for a binding site of the bitter diketopiperazine. Furthermore, affinity chromatography using cyclo(LβleucylβLβphenylalanyl) as a bitter ligand indicated that phosphoglycerides of the lipids tested showed a particular affinity to the bitter diketopiperazine.
π SIMILAR VOLUMES
## Abstract Characteristic features of a new expert system __StrucEluc__ are described. The system is intended for the structure elucidation of complex organic molecules using a variety of spectroscopic data including 2D NMR. We review here the results of challenging this system with over 100 struc