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  Adhesive barnacle peptides exhibit a steric-driven design rule to enhance adhesion between asymmetric surfaces

Raman, S., Malms, L., Utzig, T., Shrestha, B. R., Stock, P., Krishnan, S., et al. (2017). Adhesive barnacle peptides exhibit a steric-driven design rule to enhance adhesion between asymmetric surfaces. Colloids and Surfaces B, 152, 42-48. doi:10.1016/j.colsurfb.2016.12.038.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AE5A-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AE5B-2
Genre: Journal Article

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 Creators:
Raman, Sangeetha1, Author              
Malms, Lukas2, Author              
Utzig, Thomas1, Author              
Shrestha, Buddha Ratna3, Author              
Stock, Philipp1, 4, Author              
Krishnan, Shankar5, Author              
Valtiner, Markus1, 6, Author              
Affiliations:
1Interaction Forces and Functional Materials, Interface Chemistry and Surface Engineering, Max-Planck-Institut für Eisenforschung GmbH, Max Planck Society, ou_1863357              
2Department of Materials, Imperial College London, Royal School of Mines, Exhibition Road, London, UK, persistent22              
3Department of Pharmacy, University of Montreal, H3T 1J4 Montreal, Canada, ou_persistent22              
4Institut für Physikalische Chemie, der TU Bergakademie Freiberg, Leipziger Straße 29, Freiberg, Germany, persistent22              
5COMSOL Inc., 10850 Wilshire Boulevard, Suite 800, Los Angeles, CA, USA, persistent22              
6Institute for physical chemistry II, Technische Universität Bergakademie Freiberg, Leipzigerstraße 29, 09599 Freiberg, Germany , ou_persistent22              

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Free keywords: Barnacle cement; Underwater adhesive; Adhesion interface; Peptide bridging; Hydrophobic interactions; Non-covalent binding;
 Abstract: Barnacles exhibit superior underwater adhesion simply through sequencing of the 21 proteinogenic amino acids, without post processing or using special amino acids. Here, we measure and discuss the molecular interaction of two distinct and recurring short peptide sequences (Bp1 and Bp2) inspired from the surface binding 19 kDa protein from the barnacle attachment interface. Using self-assembled mono layer (SAMs) of known physical and chemical properties on molecularly smooth gold substrates in 5 mM NaCl at pH 7.3, (1) the adsorption mechanisms of the barnacle inspired peptides are explored using quartz crystal microbalance, and (2) adhesion mediating properties are measured using the surface force apparatus. The hydrophobic Bp1 peptide with a cysteine residue adsorbs irreversibly onto Au surfaces due to thiol bond formation, while on hydrophobic CH3 SAM surface, the interactions are hydrophobic in nature. Interestingly, Bp2 that contains both hydrophobic and protonated amine units exhibits asymmetric bridging with an exceptionally high adhesion energy up to 100 mJ/m(2) between mica and both gold and CH3 SAM. Surprisingly on hydrophilic surfaces such as COOH- or OH-SAMs both peptides fail to show any interactions, implying the necessity of surface charge to promote bridging. Our results provide insights into the molecular aspects of manipulating and utilizing barnacle-mediated peptides to promote or inhibit underwater adhesion. (C) 2016 Elsevier B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2017-04-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Colloids and Surfaces B
  Other : Colloids and Surfaces B-Biointerfaces
  Abbreviation : Colloids Surf., B
Source Genre: Journal
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Publ. Info: PO BOX 211, 1000 AE Amsterdam, The Netherlands : Elsevier Science BV
Pages: - Volume / Issue: 152 Sequence Number: - Start / End Page: 42 - 48 Identifier: ISSN: 0927-7765
CoNE: https://pure.mpg.de/cone/journals/resource/954926242488