蛋白质内部空间的合成模拟物：水溶性深层主体中的埋藏极性相互作用。
A synthetic mimic of protein inner space: buried polar interactions in a deep water-soluble host.
作者信息
Butterfield Sara M, Rebek Julius
机构信息
The Skaggs Institute for Chemical Biology and Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
出版信息
J Am Chem Soc. 2006 Dec 6;128(48):15366-7. doi: 10.1021/ja0663374.
A deep water-soluble cavitand was functionalized with a carboxylic acid directed toward the hydrophobic interior of the host. The buried salt-bridge interaction formed with a quinuclidium cationic guest was determined to be worth -3 kcal/mol using a free energy cycle. The strength of the interaction correlates well with buried salt bridges in proteins, indicating that the cavitand interior mimics the hydrophobic inner space of proteins.
一种水溶性深穴醚通过朝向主体疏水内部的羧酸进行功能化。利用自由能循环确定与喹核阳离子客体形成的埋藏盐桥相互作用的值为-3千卡/摩尔。这种相互作用的强度与蛋白质中的埋藏盐桥密切相关，表明穴醚内部模拟了蛋白质的疏水内部空间。
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