Molecular Conformation of Patellamide A, a Cytotoxic Cyclic Peptide from the Ascidian Lissoclinum patella, by X-Ray Crystal Analysis

Abstract

As part of a series of investigations into the conformational stability of a C₂-symmetric or related cyclic peptide isolated from the ascidian Lissoclinum patella, the molecular conformation of patellamide A, the chemical structure of which deviates slightly for C₂-symmetry, was determined by X-ray crystal analysis. Patellamide A took on a saddle-shaped rectangular form and wrapped around the water and methanol solvents. This conformation which is very similar to that of C₂-symmetric ascidiacyclamide would be proposed as a possible candidate for biologically "active" conformation.