Silk Fibroin-Based Biomaterials for Hemostatic Applications

Abstract

Hemostasis plays an essential role in all surgical procedures. Uncontrolled hemorrhage is the primary cause of death during surgeries, and effective blood loss control can significantly reduce mortality. For modern surgeons to select the right agent at the right time, they must understand the mechanisms of action, the effectiveness, and the possible adverse effects of each agent. Over the past decade, various hemostatic agents have grown intensely. These agents vary from absorbable topical hemostats, including collagen, gelatins, microfibrillar, and regenerated oxidized cellulose, to biologically active topical hemostats such as thrombin, biological adhesives, and other combined agents. Commercially available products have since expanded to include topical hemostats, surgical sealants, and adhesives. Silk is a natural protein consisting of fibroin and sericin. Silk fibroin (SF), derived from silkworm Bombyx mori, is a fibrous protein that has been used mostly in fashion textiles and surgical sutures. Additionally, SF has been widely applied as a potential biomaterial in several biomedical and biotechnological fields. Furthermore, SF has been employed as a hemostatic agent in several studies. In this review, we summarize the several morphologic forms of SF and the latest technological advances on the use of SF-based hemostatic agents.

Microporous Hemostatic Sponge Based on Silk Fibroin and Starch with Increased Structural Retentivity for Contact Activation of the Coagulation Cascade

“…The R time of this experiment would not be directly interpreted as aPTT due to the difference between measuring instruments and methods. Still, it could indicate the degree of intrinsic pathway activation like other clotting time tests targeted the intrinsic pathway with TEG. , Therefore, this result is consistent with previous studies that determined that aPTT decreased with increasing SF. , The intrinsic pathway is initiated by the clotting factor (FXII), a zymogen present in blood plasma, binding to external surfaces other than the inner blood vessel wall . Since the active site of FXII mainly contains positively charged amino acids, it likely binds to the negatively charged surface .…”

“…The intrinsic pathway is also inferred to be induced by negatively charged SF . Therefore, it is assumed that the SF component of the sponge affect the physiological hemostasis process. , However, natural hemostasis is not the only factor determining blood coagulation. As the ratio of starch increased, the blood clotting ability of SF/ST sponges quantified by BCI was improved.…”

Design of biopolymer-based hemostatic material: Starting from molecular structures and forms

“…Of note, although some studies have reported the hemostatic effect of the SF, in most cases it was combined with other components, so it is difficult to figure out the effectiveness of the SF itself. Therefore, the thorough hemostatic mechanism of the SF still needs to be comprehensively explored [ 13 , 98 ]. Keratin-based Material …”

“…Even with the same component, hemostatic materials can be prepared into different forms, e.g., powder, sponge, gauze and hydrogel, which endowed them with different hemostatic mechanisms [ 13 ]. Under different circumstances (bleeding site, depth, environment, etc), such materials have shown particular advantages for hemostasis.…”

Three-Dimensional Digital Light-Processing Bioprinting Using Silk Fibroin-Based Bio-Ink: Recent Advancements in Biomedical Applications

“…Silk fibroin (SF) is a natural polymer produced from the silkworm Bombyx mori , which was approved for use as a biomaterial in 1993 by the FDA. Recently, it has been extensively applied in the tissue engineering and biomedical fields owing to its exceptional biocompatibility, flexible mechanical properties, controlled biodegradation, and minimal propensity to invoke immune reactions [ 32 , 33 , 34 ]. SF comprises a repetition of Gly–Ala–Gly–Ala–Gly–Ser repeats of amino acid sequences, forming a β-sheet structure by self-assembly [ 35 , 36 ].…”