Mechanisms of Silk Fibroin Sol−Gel Transitions
2006
Silk fibroin sol−gel transitions were studied by monitoring the process under various physicochemical conditions with optical spectroscopy at 550 nm. The secondary structural change of the fibroin from a disordered state in solution to a β-sheet-rich conformation in the gel state was assessed by FTIR and CD over a range of fibroin concentrations, temperatures, and pH values. The structural changes were correlated to the degree of gelation based on changes in optical density at 550 nm. No detectable changes in the protein secondary structure (FTIR, CD) were found up to about 15% gelation (at 550 nm), indicating that these early stages of gelation are not accompanied by the formation of β-sheets. Above 15%, the fraction of β-sheet linearly increased with the degree of gelation. A pH dependency of gelation time was found with correlation to the predominant acidic side chains in the silk. Electrostatic interactions were related to the rate of gelation above neutral pH. The overall independencies of processing...
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