Journal
SCIENCE
Volume 348, Issue 6234, Pages 555-559Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaa7532
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Funding
- Japan Society for the Promotion of Science (JSPS) through its Funding Program for World-Leading Innovative R&D on Science and Technology (FIRST Program)
- Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan
- Platform for Drug Discovery, Informatics, and Structural Life Science from MEXT, Japan
- National Natural Science Foundation of China [21273102]
- Grants-in-Aid for Scientific Research [25000005] Funding Source: KAKEN
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Polar interactions such as electrostatic forces and hydrogen bonds play an essential role in biological molecular recognition. On a protein surface, polar interactions occur mostly in a hydrophobic environment because nonpolar amino acid residues cover similar to 75% of the protein surface. We report that ionic interactions on a hydrophobic surface are modulated by their subnanoscale distance to the surface. We developed a series of ionic head groups-appended self-assembled monolayers with C2, C6, C8, and C12 space-filling alkyl chains, which capture a dendritic guest via the formation of multiple salt bridges. The guest release upon protonolysis is progressively suppressed when its distance from the background hydrophobe changes from 1.2 (C2) to 0.2 (C12) nanometers, with an increase in salt bridge strength of similar to 3.9 kilocalories per mole.
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