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Gewählte Publikation:

Lejardi, A; Lopez, AE; Sarasua, JR; Sleytr, UB; Toca-Herrera, JL.
(2013): Making novel bio-interfaces through bacterial protein recrystallization on biocompatible polylactide derivative films
J CHEM PHYS. 2013; 139(12): FullText FullText_BOKU

Abstract:
Fabrication of novel bio-supramolecular structures was achieved by recrystallizing the bacterial surface protein SbpA on amorphous and semicrystalline polylactide derivatives. Differential scanning calorimetry showed that the glass transition temperature (T-g) for (poly-L-lactide)-PLLA, poly(L, D-lactide)-PDLLA, poly(lactide-co-glycolide)-PLGA and poly(lactide-co-caprolactone)-PLCL was 63 degrees C, 53 degrees C, 49 degrees C and 15 degrees C, respectively. Tensile stress-strain tests indicated that PLLA, PLGA, and PDLLA had a glassy behaviour when tested below Tg. The obtained Young modulus were 1477 MPa, 1330 MPa, 1306 MPa, and 9.55 MPa for PLLA, PLGA, PDLLA, and PLCL, respectively. Atomic force microscopy results confirmed that SbpA recrystallized on every polymer substrate exhibiting the native S-layer P4 lattice (a = b = 13 nm, gamma = 90 degrees). However, the polymer substrate influenced the domain size of the S-protein crystal, with the smallest size for PLLA (0.011 mu m(2)), followed by PDLLA (0.034 mu m(2)), and PLGA (0.039 mu m(2)), and the largest size for PLCL (0.09 mu m(2)). quartz crystal microbalance with dissipation monitoring (QCM-D) measurements indicated that the adsorbed protein mass per unit area (similar to 1800 ng cm(-2)) was independent of the mechanical, thermal, and crystalline properties of the polymer support. The slowest protein adsorption rate was observed for amorphous PLCL (the polymer with the weakest mechanical properties and lowest Tg). QCM-D also monitored protein self-assembly in solution and confirmed that S-layer formation takes place in three main steps: adsorption, self-assembly, and crystal reorganization. Finally, this work shows that biodegradable polylactide derivatives films are a suitable support to form robust biomimetic S-protein layers. (C) 2013 AIP Publishing LLC.
Autor*innen der BOKU Wien:
Sleytr Uwe B.
Toca-Herrera José Luis
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