SKM 2021 – scientific programme
Parts | Days | Selection | Search | Updates | Downloads | Help
DS: Fachverband Dünne Schichten
DS 4: Poster
DS 4.20: Poster
Tuesday, September 28, 2021, 10:00–13:00, P
Influence of the module number on the folding process in thin spider silk films — •Mirjam Hofmaier1,3, Birgit Urban1, Sarah Lentz4, Thomas Scheibel4, Andreas Fery1,3, and Martin Müller1,2 — 1Leibniz Institute of Polymer Research Dresden, Institute of Physical Chemistry and Polymer Physics, Hohe Str. 6, 01069 Dresden — 2Technical University Dresden, Chair of Macromolecular Chemistry, 01062 Dresden — 3Technical University Dresden, Chair of Physical Chemistry of Polymeric Materials, 01062 Dresden — 4University of Bayreuth, Chair of Biomaterials, Prof.-Rüdiger-Bormann Str. 1, 95447 Bayreuth
Aiming at a better understanding of the folding process in recombinantly produced[1], multiblockcopolymer-like spider silks, herein we report experimental work on thin films of eADF4(Cx) proteins with x = 1-16 modules. Thin eADF4(Cx) films were characterized as-cast and during methanol post-treatment (pt) using dichroic attenuated total reflection (ATR-) FTIR spectroscopy, circular dichroism (CD), and scanning force microscopy (SFM).[2]
During post-treatment, FTIR reveals an increasing β-sheet content from < 10% to > 28 % and a decreasing random coil content from > 65% to < 50%, which could be confirmed by CD analysis.[2-3] An out-of-plane orientation of the antiparallel β-sheets of the crystalline blocks could be suggested by dichroic ATR-FTIR spectroscopy.[2]
[1] D. Huemmerich et al., Biochem., 2004, 43, 13604-13612. [2] M. Hofmaier et al., JPC B, 2021, 125, 1061-1071. [3] C. Borkner et al., ACS Appl. Polym. Mater., 2019, 1, 3366-3374.