Abstract

AbstractThe utilization of silk fibroin protein (SFP) in the field of biomaterials and tissue engineering plays an important role due to its promising mechanical, biological, and processing properties. In the present study, SFP solutions were exposed to ultrasound sonication to assess impact on molecular weight (Mw), sol–gel transition behavior, and physico‐chemical properties. The Mw of SFP was significantly reduced with sonication, determined by sodium dodecyl sulfate polyacrylamide gels (SDS–PAGE) gel electrophoresis. Sol–gel transitions were observed as SFP assembled to form a reversible SFP gel network at different concentrations and sonication time with the formation of a β‐sheet‐rich conformation in the gel state. The conformational changes and morphological properties were correlated over a range of SFP concentrations by circular dichroism (CD), UV spectroscopy, swelling and attenuated total reflectance fourier transformed infrared spectroscopy (ATR‐FTIR).magnified image

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