期刊
ACS NANO
卷 11, 期 3, 页码 2586-2597出版社
AMER CHEMICAL SOC
DOI: 10.1021/acsnano.6b06360
关键词
single-molecule force spectroscopy; AFM; molecular dynamics; steered molecular dynamics; Jarzynski's equality; hydrophobic interaction; peptide; self-assembled monolayer
类别
资金
- NSF [DMR-1312548]
- German Research Foundation DFG [VA 689/3-1]
- Center for Scientific Computing at UCSB (NSF) [CNS-0960316]
- International Max Planck Research School (IMPRS) SURMAT
- National Science Foundation Graduate Research Fellowship Program [DGE 1144085]
- European Research Council [677663]
- Direct For Mathematical & Physical Scien
- Division Of Materials Research [1312548] Funding Source: National Science Foundation
- European Research Council (ERC) [677663] Funding Source: European Research Council (ERC)
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.
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