Microscopic considerations for optimizing silk biomaterials

Focus Article

Megan K. DeBari, Rosalyn D. Abbott

Published Online: Jun 25 2018

DOI: 10.1002/wnan.1534

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Silk is an especially appealing biomaterial due to its adaptable mechanical properties, allowing it to be used in a wide range of tissue engineering applications. However, processing conditions play a critical role in determining silk's mechanical properties, biodegradability, and biocompatibility. While bulk properties of silk have been widely explored, focusing on microscopic features is becoming increasingly important, as modifications at this scale largely affect the resulting regenerative properties of the biomaterial. Structural changes caused by the silk source, extraction, and processing should be carefully considered, as they will affect the biocompatibility and degradability of silk fibroin. Processing techniques and physical properties of silk that make it an ideal material for many biomedical applications will be explored.

This article is categorized under:

Implantable Materials and Surgical Technologies > Nanotechnology in Tissue Repair and Replacement
Implantable Materials and Surgical Technologies > Nanomaterials and Implants

The structure of Bombyx mori silk. Sericin covers the fibroin protein which is constructed of fibrils. A fibroin fibril consists of a heavy (~325–350 kDa) and light (~25 kDa) chain connected by a single disulfide bond. The heavy chain is composed of 12 hydrophobic repeats connected by hydrophilic linkers. Silk fibroin has a dimorphic structure with two distinct configurations, silk I and silk II. Silk I is characterized by an alpha‐helix formation, while silk II has an anti‐parallel β‐sheet nanocrystal conformation

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