Related Experiment Video
Updated: Jul 5, 2026

A High-throughput-compatible FRET-based Platform for Identification and Characterization of Botulinum Neurotoxin Light Chain Modulators
Published on: December 27, 2013
Polytheonamides A and B, highly cytotoxic, linear polypeptides with unprecedented structural features, from the
Toshiyuki Hamada1, Shigeki Matsunaga, Gen Yano
1Laboratory of Aquatic Natural Products Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
Abstract:
Polytheonamides A and B are highly cytotoxic polypeptides with 48 amino acid residues isolated from the marine sponge, Theonella swinhoei. The structure of polytheonamide B was determined by spectral and chemical methods, especially extensive 2D NMR experiments, which resulted in the unprecedented polypeptide structure; the N-terminal glycine blocked with a 5,5-dimethyl-2-oxo-hexanoyl group, the presence of eight tert-leucine, three beta-hydroxyvaline, six gamma-N-methylasparagine, two gamma-N-methyl-beta-hydroxyasparagine, and beta,beta-dimethymethionine sulfoxide residues. More significantly, it has the sequence of alternating D- and L-amino acids. Polytheonamide A is an epimer of polytheonamide B differing only in the stereochemistry of the sulfoxide of the 44(th) residue.
More Related Videos
Related Concept Videos
Physical Properties of Amines
Diversity of Protists II
Bacterial Toxins
Tetanus
Botulism
Atypical Pneumonia

