Metal-Tunable Self-Assembly of Hierarchical Structure in Mussel-Inspired Peptide Films
Source abstract
Abstract
Bottom-up control over structural hierarchy from the nanoscale through the macroscale is a critical aspect of biological materials fabrication and function, which can inspire production of advanced materials. Mussel byssal threads are a prime example of protein-based biofibers in which hierarchical organization of protein building blocks coupled via metal complexation leads to notable mechanical behaviors, such as high toughness and self-healing. Using a natural amino acid sequence from byssal thread proteins, which functions as a pH-triggered self-assembly point, we created free-standing peptide films with complex hierarchical organization across multiple length scales that can be controlled by inclusion of metal ions (Zn2+ and Cu2+) during the assembly process. Additionally, analysis of film mechanical performance indicates that metal coordination bestows up to an order of magnitude increase in material stiffness, providing a paradigm for creating tunable polymeric materials with multiscale organizational structure.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Supramolecular Self-Assembly in Materials · Bone Tissue Engineering Materials · Calcium Carbonate Crystallization and Inhibition
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Department of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam 14476, Germany
Funding
Deutsche Forschungsgemeinschaft · Max-Planck-Gesellschaft
References (38)
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