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  Targeted Tuning of Interactive Forces by Engineering of Molecular Bonds in Series and Parallel Using Peptide-Based Adhesives

Utzig, T., Stock, P., Raman, S., & Valtiner, M. (2015). Targeted Tuning of Interactive Forces by Engineering of Molecular Bonds in Series and Parallel Using Peptide-Based Adhesives. Langmuir, 31(40), 11051-11057. doi:10.1021/acs.langmuir.5b02746.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-5028-8 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-0761-9
Genre: Journal Article

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 Creators:
Utzig, Thomas1, Author              
Stock, Philipp1, Author              
Raman, Sangeetha1, Author              
Valtiner, Markus1, Author              
Affiliations:
1Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863357              

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Free keywords: Adhesive junctions; Biological process; Engineering systems; Functionalized surfaces; Interactive forces; Molecular junction; Peptide monolayers; Peptide sequences
 Abstract: Polymer-mediated adhesion plays a major role for both technical glues and biological processes like self-assembly or biorecognition. In contrast to engineering systems, adhesive strength in biological systems is precisely tuned via well-adjusted arrangement of individual bonds. How adhesion may be engineered by arrangement of individual bonds is however not yet well-understood. Here we show how the number of bonds in series and parallel can significantly influence adhesion forces using specifically designed surface-bridging peptides. We directly measure how adhesion forces between -COOH and -NH2 functionalized surfaces across aqueous media vary as a function of the number of bonds in parallel. We also introduce surface bridging peptide sequences that are similarly end-functionalized with amines and carboxylic acid. Compared to single molecular junctions, adhesive strength mediated by these surface bridging peptides decreases by a factor of 2 for adhesive junctions that consist of two acid/base bonds in series. Furthermore, adhesive strength varies with the density of bonds in parallel. For dense systems, we observe that the formation of a bridging peptide monolayer is sterically hindered and therefore adhesion is further reduced significantly by 20%. Our results unravel how the arrangement of individual bonds in an adhesive junction allows for a wide tuning of adhesive strength on the basis of utilizing just one single specific bond. As such, for peptide adhesives it is essential to consider bonds in parallel in a wide range of applications where both high adhesion and triggered release of adhesive bonds is essential.

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Language(s): eng - English
 Dates: 2015-09-182015-10-13
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

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Title: Langmuir
Source Genre: Journal
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Publ. Info: Columbus, OH : American Chemical Society
Pages: - Volume / Issue: 31 (40) Sequence Number: - Start / End Page: 11051 - 11057 Identifier: ISSN: 0743-7463
CoNE: https://pure.mpg.de/cone/journals/resource/954925541194