title: Silk fibroin solution properties related to assembly and structure.
abstract: The impact of physiological factors on silk fibroin solution properties was studied. Specifically, the impact of fibroin concentration, protein purity, cation type and concentration, and pH on aqueous solution viscosity, shear behavior, and surface tension were assessed in the context of silk protein assembly. The results demonstrate that in vitro results could be correlated to in vivo processing events during silk spinning. Rheological properties with reference to the amphiphilic block structure of the protein are described, pH dependency of shear response was quantitatively correlated to the predicted pI values of the fibroin protein, and cooperativity among environmental factors such as pH and salts was identified. Stabilization of silk fibroin solution states by calcium was identified as a mode to control shear sensitivity of the fibroin solution. The cooperativities identified suggest tight control of fibroin aqueous solution rheological properties to gain a window of protection against premature crystallization of the fibroin during processing, assuring safe storage, transport, and finally successful fiber spinning.
authors.affiliation: Department of Biomedical Engineering, Tufts University, Medford, MA 02155, USA.
authors.forename: Akira
authors.initials: A
authors.lastname: Matsumoto
authors.forename: Amil
authors.initials: A
authors.lastname: Lindsay
authors.forename: Behrouz
authors.initials: B
authors.lastname: Abedian
authors.forename: David L
authors.initials: DL
authors.lastname: Kaplan
mesh_terms: D000818:Animals; D012831:Bombyx; D005349:Fibroins / Q000096:biosynthesis / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D012212:Rheology; D012996:Solutions; D013500:Surface Tension; D014783:Viscosity
chemical_list: D012996:Solutions; D005349:Fibroins