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Engineering of the Function of Diamond-like Carbon Binding Peptides through Structural Design

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Biomacromolecules 2015, 16, 2, 476-482
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    Engineering of the Function of Diamond-like Carbon Binding Peptides through Structural Design
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    † Department of Biotechnology and Chemical Technology, Aalto University, P.O. Box 16100, 00076 Aalto, Finland
    ‡ VTT Technical Research Centre of Finland, P.O. Box 1000, 02044 VTT, Finland
    § Department of Materials Science, Aalto University, P.O. Box 11000, 00076 Aalto, Finland
    *E-mail: [email protected]. Phone: +358 50 4315525.
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    Biomacromolecules

    Cite this: Biomacromolecules 2015, 16, 2, 476–482
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    https://doi.org/10.1021/bm501522j
    Published December 18, 2014
    Copyright © 2014 American Chemical Society
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    Abstract

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    The use of phage display to select material-specific peptides provides a general route towards modification and functionalization of surfaces and interfaces. However, a rational structural engineering of the peptides for optimal affinity is typically not feasible because of insufficient structure−function understanding. Here, we investigate the influence of multivalency of diamond-like carbon (DLC) binding peptides on binding characteristics. We show that facile linking of peptides together using different lengths of spacers and multivalency leads to a tuning of affinity and kinetics. Notably, increased length of spacers in divalent systems led to significantly increased affinities. Making multimers influenced also kinetic aspects of surface competition. Additionally, the multivalent peptides were applied as surface functionalization components for a colloidal form of DLC. The work suggests the use of a set of linking systems to screen parameters for functional optimization of selected material-specific peptides.

    Copyright © 2014 American Chemical Society

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    Supporting Information

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    Information about synthesis and 1H, 13C, and 1H−1H COSY NMR spectra of PEG(6)-bis-maleimide. UPLC chromatograms and MALDI-TOF spectra of purified multivalent peptides. Fitting parameters and a plot that shows an alternative presentation of the competition curves. Amino acid sequences of control peptides. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

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    This article is cited by 4 publications.

    1. Nicolò Alvisi, Chuanbao Zheng, Meike Lokker, Victor Boekestein, Robbert de Haas, Bauke Albada, Renko de Vries. Design of Polypeptides Self-Assembling into Antifouling Coatings: Exploiting Multivalency. Biomacromolecules 2022, 23 (9) , 3507-3516. https://doi.org/10.1021/acs.biomac.2c00170
    2. Alexis de la Cotte, Cheng Wu, Marie Trévisan, Andrii Repula, and Eric Grelet . Rod-Like Virus-Based Multiarm Colloidal Molecules. ACS Nano 2017, 11 (10) , 10616-10622. https://doi.org/10.1021/acsnano.7b06405
    3. Nicolò Alvisi, Renko de Vries. Biomedical applications of solid-binding peptides and proteins. Materials Today Bio 2023, 19 , 100580. https://doi.org/10.1016/j.mtbio.2023.100580
    4. Carina Schink, Alberto Catena, Katharina Heintz, Helmar Görls, Christian Beresko, Georg Ankerhold, Marcus von der Au, Björn Meermann, Stijn J. M. Van Malderen, Frank Vanhaecke, Stefan Wehner, Wolfgang Imhof, Christian B. Fischer. Attaching Photochemically Active Ruthenium Polypyridyl Complex Units to Amorphous Hydrogenated Carbon (a-C:H) Layers. Advanced Materials Interfaces 2019, 6 (2) , 1801308. https://doi.org/10.1002/admi.201801308
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    Biomacromolecules

    Cite this: Biomacromolecules 2015, 16, 2, 476–482
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bm501522j
    Published December 18, 2014
    Copyright © 2014 American Chemical Society
    Request reuse permissions

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