Crystal structure of a peptide-steroid macrocycle - intramolecular attraction between steroids and peptidic b(I) turns.
This work describes the solid-state structure of macrocycle, contg. a steroid (lithocholic acid) and a dipeptide (Phe-Phe). The above macrocycle was obtained by the cyclodimerization of 3-(phenylalanylphenylalanylamino)lithocholic acid pentafluorophenol ester. The crystal structure of the macrocycle demonstrated that an optimal approach between the two steroidal surfaces in the mol. is achieved when the peptide parts fold to form two b(I) turns.
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