The structural basis for function in diamond-like carbon binding peptides

Bartosz Gabryelczyk, Geza Szilvay, Markus Linder (Corresponding Author)

Research output: Contribution to journalArticleScientificpeer-review

5 Citations (Scopus)

Abstract

The molecular structural basis for the function of specific peptides that bind to diamond-like carbon (DLC) surfaces was investigated. For this, a competition assay that provided a robust way of comparing relative affinities of peptide variants was set up. Point mutations of specific residues resulted in significant effects, but it was shown that the chemical composition of the peptide was not sufficient to explain peptide affinity. More significantly, rearrangements in the sequence indicated that the binding is a complex recognition event that is dependent on the overall structure of the peptide. The work demonstrates the unique properties of peptides for creating functionality at interfaces via noncovalent binding for potential applications in, for example, nanomaterials, biomedical materials, and sensors.
Original languageEnglish
Pages (from-to)8798-8802
Number of pages5
JournalLangmuir
Volume30
Issue number29
DOIs
Publication statusPublished - 2014
MoE publication typeA1 Journal article-refereed

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Diamond
Peptides
peptides
Diamonds
Carbon
diamonds
carbon
affinity
mutations
Nanostructured materials
Assays
chemical composition
sensors
Sensors
Chemical analysis

Cite this

Gabryelczyk, Bartosz ; Szilvay, Geza ; Linder, Markus. / The structural basis for function in diamond-like carbon binding peptides. In: Langmuir. 2014 ; Vol. 30, No. 29. pp. 8798-8802.
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The structural basis for function in diamond-like carbon binding peptides. / Gabryelczyk, Bartosz; Szilvay, Geza; Linder, Markus (Corresponding Author).

In: Langmuir, Vol. 30, No. 29, 2014, p. 8798-8802.

Research output: Contribution to journalArticleScientificpeer-review

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