STRUCTURE AND SUPRAMOLECULAR PACKING FEATURES OF THE DIPEPTIDE ARG-VAL ACETATE

The title compound crystallizes in the zwitterionic form. The crystal forms a supramolecular structure with the peptide molecules organized in head-to-tail columns in the b direction. The arginine side-chains a nd acetate ions interact with neighbor peptides in the c direction. In finite hydrophobic columns are present in the a direction; they involv e the valine side-chains, the acetate methyl groups and the methylene groups of the arginine side-chains. This three-dimensional organizatio n is similar to that found in Lys-Val hydrochloride. (C) Munksgaard 19 97.