2022
DOI: 10.1111/wrr.13049
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Silk proteins in reconstructive surgery: Do they possess an inherent antibacterial activity? A systematic review

Abstract: The field of reconstructive surgery encompasses a wide range of surgical procedures and regenerative approaches to treat various tissue types. Every surgical procedure is associated with the risk of surgical site infections, which are not only a financial burden but also increase patient morbidity. The surgical armamentarium in this area are biomaterials, particularly natural, biodegradable, biocompatible polymers, including the silk proteins fibroin (SF) and sericin (SS). Silk is known to be derived from silk… Show more

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Cited by 16 publications
(10 citation statements)
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“…Surgical sites are prone to infection, necessitating the use of biomaterials with antibacterial properties. 151 SBBMs have emerged as promising materials for antibacterial applications in reconstructive surgery. Cao et al developed a biocompatible surgical suture with dual light response named ZnO@SF, which exhibits rapid heating under near-infrared (NIR) light and has good antibacterial activity and controllable degradation rate.…”
Section: Biomedical Applications Of Sbbmsmentioning
confidence: 99%
See 1 more Smart Citation
“…Surgical sites are prone to infection, necessitating the use of biomaterials with antibacterial properties. 151 SBBMs have emerged as promising materials for antibacterial applications in reconstructive surgery. Cao et al developed a biocompatible surgical suture with dual light response named ZnO@SF, which exhibits rapid heating under near-infrared (NIR) light and has good antibacterial activity and controllable degradation rate.…”
Section: Biomedical Applications Of Sbbmsmentioning
confidence: 99%
“…Surgical sites are prone to infection, necessitating the use of biomaterials with antibacterial properties . SBBMs have emerged as promising materials for antibacterial applications in reconstructive surgery.…”
Section: Biomedical Applications Of Sbbmsmentioning
confidence: 99%
“…Degradation of fibroin (enzymatically, e.g., by collagenase or proteinase K) was found to depend on secondary structure, indicating that the crystalline part of fibroin (β-sheets) was more stable than the random coil part [41]. In contrast to spider silk, which is composed of 100% spidroin (main protein) with different proportions of amorphous and crystal domains [47], 60-80% of B. mori silk consists of fibroin and 15-35% of sericin [48]. Sericin has different rheological properties than fibroin [49] and forms a coating on the fibroin fibers to bind them together [15] (Figure 1).…”
Section: Structure Of Silkmentioning
confidence: 99%
“…Although some research studies have focused on a potential role for sericin, one of the components of raw silk is exposed to the elements, [18] and the results have been conflicting, [19][20][21][22] reviewed in ref. [23]. For example, the ability of raw silk fibers from silkworm cocoons to provide a substrate for limited bacterial biofilm growth was thought to protect the developing silk moth from environmental stresses.…”
Section: Introductionmentioning
confidence: 99%