Journal of Peptide Research 1997-11-01

Structure and supramolecular packing features of the dipeptide Arg-Val acetate.

R Recacha, N Verdaguer, J A Subirana

Index: J. Pept. Res. 50 , 388-392, (1997)

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Abstract

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 and acetate ions interact with neighbor peptides in the c direction. Infinite hydrophobic columns are present in the a direction; they involve the valine side-chains, the acetate methyl groups and the methylene groups of the arginine side-chains. This three-dimensional organization is similar to that found in Lys-Val hydrochloride.