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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 5: Biopolymers, Biomaterials and Bioinspired Functional Materials (joint session CPP/BP)
CPP 5.1: Vortrag
Montag, 16. März 2020, 09:30–09:45, ZEU 114
Dichroic FTIR spectrocopy on recombinant spider silk films at texturised silicon substrates — Mirjam Hofmaier1, 2, Birgit Urban1, Sarah Lentz3, Thomas Scheibel3, Andreas Fery1, 2, and •Martin Müller1, 4 — 1Leibniz-Institut für Polymerforschung Dresden e.V., Institute of Physical Chemistry and Polymer Physics, D-01069 Dresden — 2Technische Universität Dresden, Chair of Physical Chemistry of Polymeric Materials, D-01062 Dresden — 3Universität Bayreuth, Chair of Biomaterials, D-95447 Bayreuth, Germany — 4Technische Universität Dresden, Chair of Macromolecular Chemistry, D-01062 Dresden
Films of recombinant spider silk protein eADF4 were deposited onto unidirectionally scratched silicon substrates (Si-sc) and analysed by dichroic transmission (T-) and ATR-FTIR spectroscopy addressing conformation and orientation. eADF4 films (d=0-200 nm) were casted from hexafluoroisopropanol solutions onto Si-sc. Both FTIR methods revealed low b-sheet (<10%) and high random coil content (>80%) based on Amide I band analysis. Dichroic ratios R of all Amide I components close to those of isotropic samples were found by T- and ATR-FTIR indicating no eADF4 orientation. Whereas, eADF4 films after swelling in MeOH vapor revealed higher b-sheet (>30%) and lower random coil content (<60%). By ATR-FTIR high R values for the Amide I component at 1696 cm-1 assigned to antiparallel b-sheet structure were found indicating out-of-plane orientation of b-sheets, which increased with decreasing thickness. Whereas, by T-FTIR isotropic R values indicating no in-plane orientation of b-sheets were found.