Subnanoscale hydrophobic modulation of salt bridges in aqueous media

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Science  01 May 2015:
Vol. 348, Issue 6234, pp. 555-559
DOI: 10.1126/science.aaa7532

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Ions' response to hydrophobic surfaces

The strength of interactions between ions depends on their solvation environment. Schellman postulated in the 1950s that when aqueous solvated ions approached a hydrophobic surface (such as a parts of a protein surface), interactions between ions would be enhanced. Chen et al. experimentally tested this theory by studying the dissociation of organic ions bonded by salt bridges after the addition of acid. The ion pairs were held by tethers at different distances from hydrophobic surfaces. The salt bridge was stronger when it was closer to the hydrophobic surface.

Science, this issue p. 555


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 ~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 ~3.9 kilocalories per mole.

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