Bioengineering of spider silks for the production of biomedical materials

Abstract

Spider silks are well known for their extraordinary mechanical properties. This characteristic is a result of the interplay of composition, structure and self-assembly of spider silk proteins (spidroins). Advances in synthetic biology have enabled the design and production of spidroins with the aim of biomimicking the structure-property-function relationships of spider silks. Although in nature only fibers are formed from spidroins, in vitro, scientists can explore non-natural morphologies including nanofibrils, particles, capsules, hydrogels, films or foams. The versatility of spidroins, along with their biocompatible and biodegradable nature, also placed them as leading-edge biological macromolecules for improved drug delivery and various biomedical applications. Accordingly, in this review, we highlight the relationship between the molecular structure of spider silk and its mechanical properties and aims to provide a critical summary of recent progress in research employing recombinantly produced bioengineered spidroins for the production of innovative bio-derived structural materials.

Review of Spider Silk Applications in Biomedical and Tissue Engineering

“…This technique allows for the combination of spider silk proteins with various materials to create fibers with different mechanical and structural properties. Although using expression systems makes recombinant production cost-effective, the process of purifying spider silk protein powder is both time-consuming and expensive [ 67 ].…”

“…Significant progress has been made in recombinant spider silk production, but further improvements are necessary to overcome the main challenges of high investments and small product yields [ 67 ]. Additionally, the commercial use of recombinant spider silk has been limited due to the inability to produce spidroins at their natural size.…”

Progress in silk and silk fiber-inspired polymeric nanomaterials for drug delivery

“…Silk produced from spiders (spidroin proteins) are ~300 kDa and composed of a highly repetitive core, mainly consisting of alanine, glycine, and proline residues, flanked by small, nonrepetitive terminal domains, which are highly conserved across spider species (Babb et al, 2017). The development, expression, and purification of spider-inspired fibroin proteins (spidroin proteins) has been recently reviewed (Kiseleva et al, 2020;Bittencourt et al, 2022). For the purposes of this review, we focus on the nanoparticle fabrication techniques recently used in the progress toward targeted DDS, and recent publications are summarized in Table 1.…”

“…Bombyx mori silk fibroin is the most wellcharacterized silk protein source and has a variety of reactive amino acids to allow for functionalization (Murphy et al, 2008;Murphy and Kaplan, 2009;Asakura et al, 2015;Heichel and Burke, 2020;Bittencourt et al, 2022). Other silk proteins, including Bombyx mori sericin, genetically engineered silk fibroin proteins, silk fibers from other Antheraea species, and bioengineered spider fibroin silks (Bittencourt et al, 2022), are being explored due to their enhanced ability for functionalization, potential for a wider range of material and mechanical properties, and increased homogeneity of the starting polymer. In this review, we discuss the primary structure of these silk proteins and relate the structure to fabrication strategies for nanomaterials (Figure 1).…”

Self-Healing of Recombinant Spider Silk Gel and Coating

“…However, the large-scale production of spider silks faces difficulty because spiders tend to kill each other when artificial breeding is carried out in a limited space. Meanwhile, the procedure of collecting spider silks from living spiders is cost-ineffective [5]. To overcome these problems, developing artificial recombinant spider silks by genetic engineering has become a promising solution for large-scale production [3,6].…”