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Unraveling Hydrophobic Interactions at the Molecular Scale Using Force Spectroscopy and Molecular Dynamics Simulations

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Stock,  Philipp
Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society;

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Utzig,  Thomas
Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society;

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Valtiner,  Markus
Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society;
Institute for physical chemistry II, Technische Universität Bergakademie Freiberg, Leipzigerstraße 29, 09599 Freiberg, Germany ;

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Citation

Stock, P., Monroe, J. I., Utzig, T., Smith, D. J., Shell, M. S., & Valtiner, M. (2017). Unraveling Hydrophobic Interactions at the Molecular Scale Using Force Spectroscopy and Molecular Dynamics Simulations. ACS Nano, 11(3), 2586-2597. doi:10.1021/acsnano.6b06360.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-C185-E
Abstract
Interactions between hydrophobic moieties steer ubiquitous processes in aqueous media, including the self-organization of biologic matter. Recent decades have seen tremendous progress in understanding these for macroscopic hydrophobic interfaces. Yet, it is still a challenge to experimentally measure hydrophobic interactions (HIs) at the single-molecule scale and thus to compare with theory. Here, we present a combined experimental simulation approach to directly measure and quantify the sequence dependence and additivity of HIs in peptide systems at the single-molecule scale. We combine dynamic single-molecule force spectroscopy on model peptides with fully atomistic, both equilibrium and nonequilibrium, molecular dynamics (MD) simulations of the same systems. Specifically, we mutate a flexible (GS)(5) peptide scaffold with increasing numbers of hydrophobic leucine monomers and measure the peptides' desorption from hydrophobic self-assembled monolayer surfaces. Based on the analysis of nonequilibrium work-trajectories, we measure an interaction free energy that scales linearly with 3.0-3.4 k(B)T per leucine. In good agreement, simulations indicate a similar trend with 2.1 k(B)T per leucine, while also providing a detailed molecular view into HIs. This approach potentially provides a roadmap for directly extracting qualitative and quantitative single-molecule interactions at solid/liquid interfaces in a wide range of fields, including interactions at biointerfaces and adhesive interactions in industrial applications.