ICB, CNR, Department of Chemistry, University of Padova, Italy.
Chem Biol Drug Des. 2010 Feb;75(2):169-81. doi: 10.1111/j.1747-0285.2009.00920.x. Epub 2009 Dec 17.
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 alpha- 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.
中长肽（含 14 个氨基酸残基）tylopepin B 的固相合成及全化学特性表征，tylopepin B 最初从蘑菇 Tylopilus neofelleus 的子实体中提取，具有抗生素特性。这些数据伴随着通过选定的、侧链保护的片段缩合方法在溶液相中合成的结果。通过傅里叶变换红外吸收、圆二色性和二维 NMR（与分子动力学计算相结合的后一种技术）的组合使用进行的溶液构象分析，得出结论，tylopepin B 的 3D 结构在很大程度上是螺旋形的，其对 α-或 3（10）-螺旋类型的偏好取决于溶剂的性质。螺旋拓扑结构和（部分）两亲性是这种肽抗生素观察到的膜修饰特性的原因。
