Molecular conformation of patellamide A, a cytotoxic cyclic peptide from the ascidian Lissoclinum patella, by X-ray crystal analysis.
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.
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Department of Physical Chemistry, Osaka University of Pharmaceutical Sciences, Japan.
Doi
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Inoue
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Ishida
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T
Hamada
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Shioiri
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T
D000818:Animals; D018360:Crystallography, X-Ray; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D011487:Protein Conformation; D014561:Urochordata / Q000737:chemistry
D010456:Peptides, Cyclic; C085274:patellamide A