title: The structural basis for function in diamond-like carbon binding peptides.
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.
authors.affiliation: VTT Technical Research Centre of Finland , P.O. Box 1000, 02044 VTT, Finland.
authors.forename: Bartosz
authors.initials: B
authors.lastname: Gabryelczyk
authors.forename: Géza R
authors.initials: GR
authors.lastname: Szilvay
authors.forename: Markus B
authors.initials: MB
authors.lastname: Linder
mesh_terms: D000469:Alkaline Phosphatase / Q000737:chemistry / Q000235:genetics; D000595:Amino Acid Sequence; D001667:Binding, Competitive; D018130:Diamond / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D017930:Genes, Reporter; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008422:Materials Testing; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D017354:Point Mutation; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000235:genetics; D013329:Structure-Activity Relationship; D013499:Surface Properties
chemical_list: D010455:Peptides; D011993:Recombinant Fusion Proteins; D018130:Diamond; D000469:Alkaline Phosphatase