English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  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.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C193-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C194-C
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 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              

Content

show
hide
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.

Details

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

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Physical Chemistry Chemical Physics
  Abbreviation : Phys. Chem. Chem. Phys.
Source Genre: Journal
 Creator(s):
Affiliations:
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