Hydrophobic side-chain interactions in a family of dimeric amide foldamers-potential alpha-helix mimetics

被引：19
|
作者：
Kulikov, Oleg V. [1 ]
Incarvito, Christopher [1 ]
Hamilton, Andrew D. [1 ,2 ]
机构：
[1] Yale Univ, Dept Chem, New Haven, CT 06511 USA
[2] Univ Oxford, Dept Chem, Oxford OX1 3TA, England
来源：
TETRAHEDRON LETTERS | 2011年 / 52卷 / 29期
关键词：
Aromatic oligoamides; Self-assembly; Hydrophobic interactions; Helical arrangement; PROTEIN-PROTEIN INTERACTIONS; SOLID-STATE; MOLECULES;
D O I：
10.1016/j.tetlet.2011.05.004
中图分类号：
O62 [有机化学];
学科分类号：
070303 ; 081704 ;
摘要：
A series of new alpha-helix mimetics based on a benzamide scaffold and potentially able to disrupt protein-protein interactions have been synthesized and characterized by X-ray analysis. Inspection of the solid state structures of aromatic amide dimers confirmed that the molecules adopt a curved conformation with intramolecular H-bonding between the amide NH and the alkoxy oxygen of the neighboring aromatic fragment (d(NH center dot center dot center dot O) similar to 2 angstrom). Adjacent dimer molecules are prone to form supramolecular assemblies due to both hydrophobic alkyl side-chain/side-chain interactions and intermolecular H-bonding. (C) 2011 Elsevier Ltd. All rights reserved.
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页码：3705 / 3709
页数：5
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