Mechanisms of silk fibroin sol-gel transitions.
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 beta-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 beta-sheets. Above 15%, the fraction of beta-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 parameters including concentration, temperature, and pH on gel formation and protein structure can be related to primary sequence-specific features in the molecular organization of the fibroin protein. These findings clarify aspects of the self-assembly of this unique family of proteins as a route to gain control of material properties, as well as for new insight into the design of synthetic silk-biomimetic polymers with predictable solution and assembly properties.
Matsumoto
Akira
A
Department of Biomedical Engineering, Chemical and Biological Engineering, Bioengineering & Biotechnology Center, Tufts University, Medford, Massachusetts 02155, USA.
Chen
Jingsong
J
Collette
Adam L
AL
Kim
Ung-Jin
UJ
Altman
Gregory H
GH
Cebe
Peggy
P
Kaplan
David L
DL
D005349:Fibroins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D015394:Molecular Structure; D044367:Phase Transition
D005349:Fibroins