Engineering of the function of diamond-like carbon binding peptides through structural design

Bartosz Gabryelczyk, Géza R. Szilvay, Vivek K. Singh, Joona Mikkilä, Mauri A. Kostiainen, Jari Koskinen, Markus B. Linder (Corresponding Author)

    Research output: Contribution to journalArticleScientificpeer-review

    2 Citations (Scopus)

    Abstract

    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.
    Original languageEnglish
    Pages (from-to)476-482
    JournalBiomacromolecules
    Volume16
    Issue number2
    DOIs
    Publication statusPublished - 2015
    MoE publication typeA1 Journal article-refereed

    Keywords

    • peptides
    • surfaces
    • interfaces
    • diamond-like carbon
    • functional optimization

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