β-Sheet Structure Formation within Binary Blends of Two Spider Silk Related Peptides
Hofmaier M, Malanin M, Bittrich E, Lentz S, Urban B, Scheibel T, Fery A, Mueller M (2023)
Publication Type: Journal article
Publication year: 2023
Journal
Book Volume: 24
Pages Range: 825-840
Journal Issue: 2
DOI: 10.1021/acs.biomac.2c01266
Abstract
Intrinsically disordered proteins (IDPs) play an important role in molecular biology and medicine because their induced folding can lead to so-called conformational diseases, where β-amyloids play an important role. Still, the molecular folding process into the different substructures, such as parallel/antiparallel or extended β-sheet/crossed β-sheet is not fully understood. The recombinant spider silk protein eADF4(Cx) consisting of repeating modules C, which are composed of a crystalline (pep-c) and an amorphous peptide sequence (pep-a), can be used as a model system for IDP since it can assemble into similar structures. In this work, blend films of the pep-c and pep-a sequences were investigated to modulate the β-sheet formation by varying the molar fraction of pep-c and pep-a. Dichroic Fourier-transform infrared spectroscopy (FTIR), circular dichroism, spectroscopic ellipsometry, atomic force microscopy, and IR nanospectroscopy were used to examine the secondary structure, the formation of parallel and antiparallel β-sheets, their orientation, and the microscopic roughness and phase formation within peptide blend films upon methanol post-treatment. New insights into the formation of filament-like structures in these silk blend films were obtained. Filament-like structures could be locally assigned to β-sheet-rich structures. Further, the antiparallel or parallel character and the orientation of the formed β-sheets could be clearly determined. Finally, the ideal ratio of pep-a and pep-c sequences found in the fibroin 4 of the major ampullate silk of spiders could also be rationalized by comparing the blend and spider silk protein systems.
Involved external institutions
Germany (DE)How to cite
APA:
Hofmaier, M., Malanin, M., Bittrich, E., Lentz, S., Urban, B., Scheibel, T.,... Mueller, M. (2023). β-Sheet Structure Formation within Binary Blends of Two Spider Silk Related Peptides. Biomacromolecules, 24(2), 825-840. https://doi.org/10.1021/acs.biomac.2c01266
MLA:
Hofmaier, Mirjam, et al. "β-Sheet Structure Formation within Binary Blends of Two Spider Silk Related Peptides." Biomacromolecules 24.2 (2023): 825-840.
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