An exceptionally stable peptide nanotube system with flexible pores

被引:83
作者
Görbitz, CH [1 ]
机构
[1] Univ Oslo, Dept Chem, N-0315 Oslo, Norway
来源
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE | 2002年 / 58卷
关键词
D O I
10.1107/S0108768102012314
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The hydrophobic channels in the structure of the dipeptide L-alanyl-L-valine act as supramolecular hosts for organic solvent molecules. In a series of data collections, it is demonstrated that small molecules like acetonitrile, methanol and acetone can be removed from the channels by drying without impairing the structure of the hydrogen-bonded peptide host structure. The title compound is one of the very first organic molecules to be found to have this property. Alcohol guests larger than methanol are also absorbed, but they induce a doubling of two axes and a change in the shape and size of the pores. The observed structural modifications explain why these solvent molecules are more or less irreversibly trapped inside the channels.
引用
收藏
页码:849 / 854
页数:6
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