Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 37, Pages 12941-12945Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja104616z
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Funding
- Ministry of Education, Science, and Culture of Japan
- Volkswagen Foundation
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Polytheonamide B (pTB), a highly cytotoxic polypeptide, is one of the most unusual nonribosomal peptides of sponge origin. pTB is a linear 48-residue peptide with alternating D- and L-amino acids and contains a total of eight types of nonproteinogenic amino acids. To investigate the mechanisms underlying its cytotoxic activity, we determined the three-dimensional structure of pTB by NMR spectroscopy, structure calculation, and energy minimization. pTB adopts a single right-handed beta(6.3)-helical structure in a 1:1 mixture of methanol/chloroform with a length of approximately 45 angstrom and a hydrophilic pore of ca. 4 angstrom inner diameter. These features indicate that pTB molecules form transmembrane channels that permeate monovalent cations as gramicidin A channels do. The strong cytotoxicity of pTB can be ascribed to its ability to form single molecule channels through biological membranes.
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