Dresden 2020 – scientific programme
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CPP: Fachverband Chemische Physik und Polymerphysik
CPP 24: Poster Session I
CPP 24.4: Poster
Monday, March 16, 2020, 17:30–19:30, P3
Folding kinetics within recombinant spider silk coatings — •Mirjam Hofmaier1, 2, Birgit Urban1, Sarah Lentz3, Thomas Scheibel3, Andreas Fery1, 2, and Martin Müller4 — 1Leibniz Institute of Polymer Research Dresden, Institute of Physical Chemistry and Polymer Physics, Hohe Straße 6, D-01069 Dresden — 2Technical University Dresden, Chair of Physical Chemistry of Polymeric Materials, 01069 Dresden — 3University of Bayreuth, Chair of Biomaterials, Rüdiger-Bormann Str. 1, D-95447 Bayreuth — 4Technical University Dresden, Chair of Macromolecular Chemistry, 01062 Dresden
The folding kinetics of the recombinant spider silk protein eADF4(C16) in thin films was analysed by in-situ ATR-FTIR spectroscopy. eADF4(C16) was cast from hexafluoroisopropanol solutions (1-50 mg/ml) to respective thin and thick films onto unidirectionally scratched silicon substrates (Si-sc). To quantify secondary structure portions, the Amide-I band was examined using line shape analysis (LSA). Five relevant components in the range between 1585 and 1730 cm-1 were identified and assigned to typical secondary structures. Significant decrease of random coil and increase of beta-sheet content was recorded by ATR-FTIR measurements over 24 hours while treating the initial eADF4(C16) films with methanol vapour (MeOH-v) or liquid methanol (MeOH-l). The protein folding appears to be a two-state kinetic process. Received rate constants indicate folding kinetics of first order by MeOH-v treatment and both zero and first order by MeOH-l treatment. No dependence of folding kinetics on the layer thickness could be found.