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)

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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

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Keywords

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

Cite this

Gabryelczyk, B., Szilvay, G. R., Singh, V. K., Mikkilä, J., Kostiainen, M. A., Koskinen, J., & Linder, M. B. (2015). Engineering of the function of diamond-like carbon binding peptides through structural design. Biomacromolecules, 16(2), 476-482. https://doi.org/10.1021/bm501522j