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Synthesis, Preferred Conformation, and Membrane Activity of Medium‐Length Peptaibiotics: Tylopeptin B
Author(s) -
Gobbo Marina,
Poloni Claudia,
De Zotti Marta,
Peggion Cristina,
Biondi Barbara,
Ballano Gema,
Formaggio Fernando,
Toniolo Claudio
Publication year - 2010
Publication title -
chemical biology and drug design
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.59
H-Index - 77
eISSN - 1747-0285
pISSN - 1747-0277
DOI - 10.1111/j.1747-0285.2009.00920.x
Subject(s) - circular dichroism , helix (gastropod) , side chain , chemistry , crystallography , membrane , stereochemistry , solvent , organic chemistry , polymer , biochemistry , biology , ecology , snail
The solid‐phase synthesis and full chemical characterization of the medium‐length (14‐amino acid residues) peptaibol with antibiotic properties of tylopeptin B, originally extracted from the fruiting body of the mushroom Tylopilus neofelleus , are described. These data are accompanied by the results on the solution‐phase synthesis via the segment condensation approach of a selected, side‐chain protected, analog. A solution conformational analysis, performed by the combined use of FTIR absorption, circular dichroism, and 2D‐NMR (the latter technique coupled to molecular dynamics calculations), favors the conclusion that the 3D‐structure of tylopeptin B is largely helical with a preference for the α‐ or the 3 10 ‐helix type depending upon the nature of the solvent. Helix topology and (partial) amphiphilic character are responsible for the observed membrane‐modifying properties of this peptaibiotic.