Biomacromolecules · 2008 · 11 citations · 28 references
Natural SciencesChemistryMaterials ScienceBiomaterialsPolymer ChemistrySurface ScienceBiodegradable PolymersPolymer AdhesionPolymer CharacterizationPolymer StructurePolymer SurfacesProtein AdsorptionAdsorbent InteractionsAdsorption At Polymer InterfacesDepolymerizationPolymer AdsorptionPolymer Surface ChemistryPotential Energy LandscapeSubstrate Binding DynamicsSubstrate Binding Sites
Molecular recognition of poly[(R)-3-hydroxybutyrate] (P(3HB)) depolymerase from Ralstonia pickettii T1 to the surfaces of biodegradable aliphatic polyesters such as P(3HB) and poly(L-lactic acid) (PLLA) was examined from the viewpoints of kinetics and dynamics. To determine the kinetic parameters on the interaction between the substrate-binding domain (SBD) of P(3HB) depolymerase and various polymer substrates with different chemical structures, surface plasmon resonance (SPR) measurements were performed. On the other hand, using an atomic force microscopic (AFM) cantilever tip functionalized with the SBD of P(3HB) depolymerase, the mechanical parameters such as unbinding force to the polymer surfaces were measured. Both the SPR and AFM measurements showed that the SBD has a high affinity to P(3HB) and PLLA. From the results of kinetics and dynamics, the energy potential landscape of SBD-polymer interaction was disclosed on the basis of a phenomenological model, and the mechanism of the interaction was discussed.
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