Biomimicking Materials

Biomimicking Materials

Biological assemblies therefore share properties with synthetic materials denoted “soft matter”, i.e. they are fluctuating, susceptible to external fields and follow the same physics as synthetic analogs such as surfactants, polymers and colloids. While regular synthetic amphiphiles readily form well-defined (e.g. spherical, cylindrical) nanostructures, they lack the structural specificity and encoded biological function found for proteins, which consist of well-defined amino acid sequences.

The potential of mimicking natural protein-based materials and control their function using fully synthetic materials is strongly appealing for many biomedical and nanotechnological applications. The current bottleneck in this field is not necessarily synthetic methods; the recent decade has seen a significant development in synthesis of hybrid systems involving biological building blocks such as peptides, proteins and lipids, or peptidomimetics such as peptoids (poly-N-substituted glycines).  For a full application of such systems, the design rules for both spontaneous and guided formation must be known. This requires fundamental insight into their thermodynamics, kinetic pathways of formation, dynamics and response towards external perturbation.

Active group members
  • PhD student Nico König
  • Post Doc Matthias Amann
Publications
  • Sun, J. et al. Self-assembly of crystalline nanotubes from monodisperse amphiphilic diblock copolypeptoid tiles. Proceedings of the National Academy of Sciences 113, 3954–3959 (2016).
  • Xu, D. et al. Toward hemocompatible self-assembling antimicrobial nanofibers: understanding the synergistic effect of supramolecular structure and PEGylation on hemocompatibility. RSC Adv. 6, 15911–15919 (2016).
  • Jiang, L. et al. Protein‐like Nanoparticles Based on Orthogonal Self‐Assembly of Chimeric Peptides. Small (2016). doi:10.1002/smll.201600910
  • Sun, J. et al. Self-assembly of crystalline nanotubes from monodisperse amphiphilic diblock copolypeptoid tiles. Proceedings of the National Academy of Sciences 113, 3954–3959 (2016).
  • Ang, J. C., Ma, D., Lund, R., Keten, S. & Xu, T. Internal structure of 15 nm 3-helix micelle revealed by small-angle neutron scattering and coarse-grained MD simulation. Biomacromolecules 17, 3262–3267 (2016).
  • Lund, R., Ang, J. C., Shu, J. Y. & Xu, T. Understanding Peptide Oligomeric State in Langmuir Monolayers of Amphiphilic 3-Helix Bundle-Forming Peptide-PEG Conjugates. Biomacromolecules 17, 3964–3972 (2016).
  • Dong, H., Lund, R. & Xu, T. Micelle Stabilization via Entropic Repulsion: Balance of Force Directionality and Geometric Packing of Subunits. Biomacromolecules 16, 743–747 (2015).
  • Xu, D. et al. Designed supramolecular filamentous peptides: balance of nanostructure, cytotoxicity and antimicrobial activity. Commun. 51, 1289–1292 (2014).
  • Yang, M. et al. Filamentous supramolecular peptide–drug conjugates as highly efficient drug delivery vehicles. Commun. 50, 4827–4830 (2014).
  • Lund, R., Shu, J. & Xu, T. A Small-Angle X-ray Scattering Study of α-helical Bundle-Forming Peptide–Polymer Conjugates in Solution: Chain Conformations. Macromolecules 46, 1625–1632 (2013).