Abstract
Biological self-assembly is a process in which building blocks autonomously organize to form stable supermolecules of higher order and complexity through domination of weak, noncovalent interactions. For silk protein, the effect of high incubating temperature on the induction of secondary structure and self-assembly was well investigated. However, the effect of freezing and thawing on silk solution has not been studied. The present work aimed to investigate a new all-aqueous process to form 3D porous silk fibroin matrices using a freezing-assisted self-assembly method. This study proposes an experimental investigation and optimization of environmental parameters for the self-assembly process such as freezing temperature, thawing process, and concentration of silk solution. The optical images demonstrated the possibility and potential of −80ST48 treatment to initialize the self-assembly of silk fibroin as well as controllably fabricate a porous scaffold. Moreover, the micrograph images illustrate the assembly of silk protein chain in 7 days under the treatment of −80ST48 process. The surface morphology characterization proved that this method could control the pore size of porous scaffolds by control of the concentration of silk solution. The animal test showed the support of silk scaffold for cell adhesion and proliferation, as well as the cell migration process in the 3D implantable scaffold.
Highlights
Self-assembly is a process by which components spontaneously form a well-defined stable structure under several certain conditions
To investigate the effect of thawing on the self-assembly at different freezing temperatures, the designed immediate thawing (IT), ST24, and ST48 processes were applied to 6% silk solution at −20∘C and −80∘C
Both −20IT and −80IT samples returned to the initial solution state, which had no visible difference with the control group
Summary
Self-assembly is a process by which components spontaneously form a well-defined stable structure under several certain conditions. This process is scattered in natural systems (e.g., secondary and higher order structures of protein) and is investigated for engineered systems as a promising method to fabricate supermolecular architecture and harness biomaterial properties from the bottom up [1,2,3,4]. The number of studies focusing on silk protein investigation and silk-based material production based on its natural self-assembly property is remarkable [5,6,7,8].
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