A synthetic mimic of protein inner space: buried polar interactions in a deep water-soluble host.
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.
Butterfield
Sara M
SM
The Skaggs Institute for Chemical Biology and Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Rebek
Julius
J
D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D014867:Water / Q000737:chemistry*
D011506:Proteins; D014867:Water