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  Soft matter interactions at the molecular scale: interaction forces and energies between single hydrophobic model peptides

Stock, P., Utzig, T., & Valtiner, M. (2017). Soft matter interactions at the molecular scale: interaction forces and energies between single hydrophobic model peptides. Physical Chemistry Chemical Physics, 19(6), 4216-4221. doi:10.1039/c6cp07562b.

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 Creators:
Stock, Philipp1, 2, Author           
Utzig, Thomas2, Author           
Valtiner, Markus2, 3, Author           
Affiliations:
1Institut für Physikalische Chemie, der TU Bergakademie Freiberg, Leipziger Straße 29, Freiberg, Germany, persistent22              
2Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863357              
3Institute for physical chemistry II, Technische Universität Bergakademie Freiberg, Leipzigerstraße 29, 09599 Freiberg, Germany , ou_persistent22              

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Free keywords: NONEQUILIBRIUM MEASUREMENTS; LONG-RANGE; SPECTROSCOPY; MICROSCOPY; ADHESION; INTERFACES; CHEMISTRY; STRENGTH; BONDS
 Abstract: In all realms of soft matter research a fundamental understanding of the structure/property relationships based on molecular interactions is crucial for developing a framework for the targeted design of soft materials. However, a molecular picture is often difficult to ascertain and yet essential for understanding the many different competing interactions at play, including entropies and cooperativities, hydration effects, and the enormous design space of soft matter. Here, we characterized for the first time the interaction between single hydrophobic molecules quantitatively using atomic force microscopy, and demonstrated that single molecular hydrophobic interaction free energies are dominated by the area of the smallest interacting hydrophobe. The interaction free energy amounts to 3-4 kT per hydrophobic unit. Also, we find that the transition state of the hydrophobic interactions is located at 3 A with respect to the ground state, based on Bell-Evans theory. Our results provide a new path for understanding the nature of hydrophobic interactions at the single molecular scale. Our approach enables us to systematically vary hydrophobic and any other interaction type by utilizing peptide chemistry providing a strategic advancement to unravel molecular surface and soft matter interactions at the single molecular scale.

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Language(s): eng - English
 Dates: 2017-02-14
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000395526600006
DOI: 10.1039/c6cp07562b
 Degree: -

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Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
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Publ. Info: Cambridge, England : Royal Society of Chemistry
Pages: - Volume / Issue: 19 (6) Sequence Number: - Start / End Page: 4216 - 4221 Identifier: ISSN: 1463-9076
CoNE: https://pure.mpg.de/cone/journals/resource/954925272413_1