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Inhibition of Ice Recrystallization by Nanotube-Forming Cyclic Peptides
Romà Surís-Valls1,2,3, Tim P Hogervorst1,2, Sandra M C Schoenmakers2
1Laboratory of Self-Organizing Soft Matter, Department of Chemical Engineering and Chemistry, Eindhoven University of Technology, 5600 MB Eindhoven, The Netherlands.
Biomacromolecules
|January 20, 2022
Summary
Researchers created rigid, artificial ice-binding nanotubes from cyclic peptides. These nanotubes show pH-dependent ice recrystallization inhibition activity, offering a novel approach to biomaterial design.
Area of Science:
- Biomaterials Science
- Protein Engineering
- Supramolecular Chemistry
Background:
- Native ice-binding proteins are typically rigid, while synthetic ice-binders are often flexible, posing challenges for precise motif arrangement.
- Designing synthetic ice-binders with regular arrays of ice-binding motifs is difficult.
Purpose of the Study:
- To develop large, rigid, artificial ice-binders using self-assembling cyclic peptides.
- To incorporate insect-derived ice-binding motifs into synthetic structures.
- To investigate the self-assembly and ice-binding activity of these novel constructs.
Main Methods:
- Design, synthesis, and purification of cyclic octapeptide Lys2CP8 using Fmoc chemistry and HPLC.
- Characterization of self-assembly using circular dichroism (CD) spectroscopy, Fourier-transform infrared (FTIR) spectroscopy, and light scattering (LS).
- Visualization of nanostructure using cryogenic transmission electron microscopy (cryo-TEM).
- Assessment of ice recrystallization inhibition (IRI) activity at different pH levels.
Main Results:
- Lys2CP8 self-assembled into nanoscopic objects in a pH- and concentration-dependent manner.
- FTIR and CD spectroscopy indicated the formation of intermolecular antiparallel β-sheets in aggregates.
- Cryo-TEM confirmed the presence of one-dimensional nanotube structures, which were well-dispersed at pH 3 and bundled at pH 11.
- Ice recrystallization inhibition (IRI) activity was observed at pH 3 but not at pH 11, correlating with the observed assembly behavior.
Conclusions:
- Cyclic peptides can be engineered into rigid, self-assembling ice-binding nanotubes.
- The pH-dependent assembly of Lys2CP8 influences its ice-binding activity.
- This work presents a promising strategy for creating tunable, artificial ice-binding materials.
