Abstract
Self-assembled peptide/protein nanofibers are valuable 1D building blocks for creating complex structures with designed properties and functions. It is reported that the self-assembly of silk-elastin-like protein polymers into nanofibers or globular aggregates in aqueous solutions can be modulated by tuning the temperature of the protein solutions, the size of the silk blocks, and the charge of the elastin blocks. A core-sheath model is proposed for nanofiber formation, with the silk blocks in the cores and the hydrated elastin blocks in the sheaths. The folding of the silk blocks into stable cores - affected by the size of the silk blocks and the charge of the elastin blocks - plays a critical role in the assembly of silk-elastin nanofibers. Furthermore, enhanced hydrophobic interactions between the elastin blocks at elevated temperatures greatly influence the nanoscale features of silk-elastin nanofibers. Silk-elastin-like protein polymers are capable of self-assembling into nanofibers in aqueous solutions. The self-assembly of silk-elastin nanofibers can be tuned by the assembling temperature of protein solutions, the size of the silk blocks, and the charges of the elastin blocks. A core-sheath model is proposed for the process of silk-elastin nanofiber formation.
Original language | English (US) |
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Pages (from-to) | 1273-1279 |
Number of pages | 7 |
Journal | Macromolecular Rapid Communications |
Volume | 35 |
Issue number | 14 |
DOIs | |
State | Published - Jul 2014 |
Keywords
- aqueous self-assembly
- nanofibers
- polypeptide sequences
- silk-elastin-like proteins
- temperature sensitive
ASJC Scopus subject areas
- Materials Chemistry
- Polymers and Plastics
- Organic Chemistry