The ratio of fibroin to sericin in the middle silk gland of Bombyx mori and its correlation with the extensional behavior of the silk dope.

Understanding how native silk spinning occurs is crucial for designing artificial spinning systems. One often overlooked factor in Bombyx mori is the secretion of sericin proteins. Herein, we investigate the variation in amino acid content at different locations in the middle silk gland (MSG) of B. mori. This variation corresponds to an increase in sericin content when moving towards the anterior region of the MSG, while the posterior region predominantly contains fibroin. We estimate the mass ratio of sericin to fibroin to be ~25/75 wt% in the anterior MSG, depending on the fitting method. Then, we demonstrate that the improvement in the extensional behavior of the silk dope in the MSG correlates with the increase in sericin content. The addition of sericin may decrease the viscosity of the silk dope, a factor associated with an increase in the spinnability of silk. We further discuss whether this effect could also result from other known physicochemical changes within the MSG.

Pulling and analyzing silk fibers from aqueous solution using a robotic device.

Spiders, silkworms, and many other animals can spin silk with exceptional properties. However, artificially spun fibers often fall short of their natural counterparts partly due sub-optimal production methods. A variety of methods, such as wet-, dry-, and biomimetic spinning have been used. The methods are based on extrusion, whereas natural spinning also involves pulling. Another shortcoming is that there is a lack feedback control during extension. Here we demonstrate a robotic fiber pulling device that enables controlled pulling of silk fibers and in situ measurement of extensional forces during the pulling and tensile testing of the pulled fibers. The pulling device was used to study two types of silk-one recombinant spider silk (a structural variant of ADF3) and one regenerated silk fibroin. Also, dextran-a branched polysaccharide-was used as a reference material for the procedure due to its straightforward preparation and storage. No post-treatments were applied. The pulled regenerated silk fibroin fibers achieved high tensile strength in comparison to similar extrusion-based methods. The mechanical properties of the recombinant spider silk fibers seemed to be affected by the liquid-liquid phase separation of the silk proteins.

Shaping Liquid Droplets on an Active Air-Ferrofluid Interface.

An air-liquid interface is important in many biological and industrial applications, where the manipulation of liquids on the air-liquid interface can have a significant impact. However, current manipulation techniques on the interface are mostly limited to transportation and trapping. Here, we report a magnetic liquid shaping method that can squeeze, rotate, and shape nonmagnetic liquids on an air-ferrofluid interface with programmable deformation. We can control the aspect ratio of the ellipse and generate repeatable quasi-static shapes of a hexadecane oil droplet. We can rotate droplets and stir liquids into spiral-like structures. We can also shape phase-changing liquids and fabricate shape-programmed thin films at the air-ferrofluid interface. The proposed method may potentially open up new possibilities for film fabrication, tissue engineering, and biological experiments that can be carried out at an air-liquid interface.

Highly Hydrophobic Films of Engineered Silk Proteins by a Simple Deposition Method.

Molecular engineering of protein structures offers a uniquely versatile route for novel functionalities in materials. Here, we describe a method to form highly hydrophobic thin films using genetically engineered spider silk proteins. We used structurally engineered protein variants containing ADF3 and AQ12 spider silk sequences. Wetting properties were studied using static and dynamic contact angle measurements. Solution conditions and the surrounding humidity during film preparation were key parameters to obtain high hydrophobicity, as shown by contact angles in excess of 120°. Although the surface layer was highly hydrophobic, its structure was disrupted by the added water droplets. Crystal-like structures were found at the spots where water droplets had been placed. To understand the mechanism of film formation, different variants of the proteins, the topography of the films, and secondary structures of the protein components were studied. The high contact angle in the films demonstrates that the conformations that silk proteins take in the protein layer very efficiently expose their hydrophobic segments. This work reveals a highly amphiphilic nature of silk proteins and contributes to an understanding of their assembly mechanisms. It will also help in designing diverse technical uses for recombinant silk.