| 词条 | Fibroin |
| 释义 |
The fibroin protein consists of layers of antiparallel beta sheets. Its primary structure mainly consists of the recurrent amino acid sequence (Gly-Ser-Gly-Ala-Gly-Ala)n. The high glycine (and, to a lesser extent, alanine) content allows for tight packing of the sheets, which contributes to silk's rigid structure and tensile strength. A combination of stiffness and toughness make it a material with applications in several areas, including biomedicine and textile manufacture. Fibroin is known to arrange itself in three structures, called silk I, II, and III. Silk I is the natural form of fibroin, as emitted from the Bombyx mori silk glands. Silk II refers to the arrangement of fibroin molecules in spun silk, which has greater strength and is often used in various commercial applications. Silk III is a newly discovered structure of fibroin.[3] Silk III is formed principally in solutions of fibroin at an interface (i.e. air-water interface, water-oil interface, etc.). DegradationMany species of Amycolatopsis and Saccharotrix bacteria are able to degrade both silk fibroin and polylactic acid.[4] References1. ^O. Hakimi et al., “Spider and mulberry silkworm silks as compatible biomaterials”,Composites Part B: Engineering, vol. 38 (3), pp. 324--337, article {{DOI|10.1016/j.compositesb.2006.06.012}} 2. ^T. Dyakonov et al., “Design and Characterization of a Silk-Fibroin-Based Drug Delivery Platform Using Naproxen as a Model Drug”, Journal of Drug Delivery, vol. 2012 (2012), article ID 490514 3. ^{{cite journal | doi = 10.1016/S0141-8130(99)00002-1 | title = Orientation of silk III at the air-water interface | journal = International Journal of Biological Macromolecules | volume = 24 | issue = 2–3 | year = 1999 |pages = 237–242 | first1 = Regina | last1 = Valluzzi| first2 =Samuel P. | last2 =Gido| first3 =Wayne | last3 =Muller| first4 =David L. | last4 =Kaplan}} 4. ^{{cite journal|title=Biodegradability of Plastics|journal=International Journal of Molecular Sciences|author1=Yutaka Tokiwa|author2=Buenaventurada P. Calabia|author3=Charles U. Ugwu|author4=Seiichi Aiba|pages=3722–3742|date=September 2009|volume=10|issue=9|pmc=2769161|pmid=19865515|doi=10.3390/ijms10093722}} 2 : Animal proteins|Silk |
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