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A novel and selective silk fibroin fragmentation method.

Francesca Agostinacchio¹, Devid Maniglio¹, Emanuela Callone²

¹Department of Industrial Engineering, University of Trento, via Sommarive 9, Trento, Italy. antonella.motta@unitn.it f.agostinacchio@unitn.it devid.maniglio@unitn.it emanuela.callone@unitn.it claudio.migliaresi@unitn.it sandra.dire@unitn.it and BIOTech Research Center, European Institute of Excellence on Tissue Engineering and Regenerative Medicine, University of Trento, via delle Regole 101, Trento, Italy.

|July 6, 2021

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Researchers precisely fragmented silk fibroin using enzymes to create tunable, lower molecular weight biomaterials. This method enhances reactivity and stability for advanced tissue engineering applications.

Area of Science:

Biomaterials Science
Tissue Engineering
Polymer Chemistry

Background:

Silk fibroin is a versatile biomaterial in tissue engineering.
Tailoring silk fibroin's molecular weight and structure is crucial for specific applications.
Current methods for modifying silk fibroin have limitations.

Purpose of the Study:

To develop a precise and tunable method for reducing silk fibroin's molecular weight.
To investigate the impact of enzymatic fragmentation on silk fibroin's properties.
To create a novel silk-derived material with enhanced characteristics for bioengineering.

Main Methods:

Selective enzymatic cleavage of the silk fibroin chain at specific amino acid sites.
Tuning molecular weight and properties by controlling enzyme concentration.

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Characterization of fragmented fibroin using structural and thermal analyses (e.g., FTIR, DSC).

Preparation and analysis of fragmented silk fibroin films.

Main Results:

Enzymatic fragmentation precisely reduced silk fibroin molecular weight.
Increased presence of free amino groups, enhancing reactivity.
Aqueous solutions of fragmented fibroin remained stable for up to seven days.
Fragmentation did not impede beta-sheet formation post-methanol treatment.
Differences in secondary structure rearrangements were observed after water-vapor annealing.

Conclusions:

Enzymatic fragmentation offers a fast, controllable, and precise method for silk fibroin modification.
The resulting silk-derived material is stable in water with tunable molecular weight and secondary structure.
This approach provides a versatile tool for modulating bioengineered constructs in tissue engineering.