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2012 - Selective modification of the N-Terminal structure of polytheonamide B significantly changes its cytotoxicity and activity as an ion channel

icon pap   Port-a-Patch publication in ChemMedChem (2012)

Authors: 
Shinohara N., Itoh H., Matsuoka S., Inoue M.

 

Journal: 
ChemMedChem (2012) 7(10):1770–1773


Abstract: 

Chemical point mutation: Polytheonamide B is a naturally occurring polypeptide containing 48 amino acids. It both displays potent cytotoxicity and acts as a monovalent cation channel in vitro. Chemoselective methods to modify the 44th, N-, and C-terminal residues of the natural product have been developed, and evaluation of the resultant derivatives suggests that the intrinsic activities of the peptide can only be altered by switching its N-terminal substitution.


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