Fibroin

Fibroin light chain
other names	L-fibroin, fibroin light chain
Mass / length primary structure	262 amino acids , 27,669 Da
Identifier
External IDs	UniProt : P21828 ;

Fibroin heavy chain
other names	H-fibroin, fibroin heavy chain
	Existing structure data : PDB 3UA0
Mass / length primary structure	5,263 amino acids , 391,593 Da
Identifier
External IDs	UniProt : P05790 ;

Fibroin is a fiber protein and as such the main component of silk . It is secreted by various silk spinners in the course of the production of silk fibers in special glands or epithelia .

properties

Repeat unit of the fibroin

Fibroin is a heterodimer made up of two subunits, of which the heavy chain with 5,263 amino acids is a large subunit compared to other proteins . It has repeating units. Silk thread consists of two filaments of fibroin covered with sericin . Fibroin can exist in three structures, Fibroin I to III. The silk of Bombyx mori corresponds to Type I. Type II generated during spinning of silk proteins and type III is at interfaces formed.

Fibroin is being studied for use as a biomaterial .

literature

M. Andersson, J. Johansson, A. Rising: Silk Spinning in Silkworms and Spiders. In: International journal of molecular sciences. Volume 17, number 8, August 2016, p., Doi : 10.3390 / ijms17081290 , PMID 27517908 , PMC 5000687 (free full text).

Individual evidence

↑ Osnat Hakimi, David P. Knight, Fritz Vollrath, Pankaj Vadgama: Spider and mulberry silkworm silks as compatible biomaterials. In: Composites Part B: Engineering. 38, 2007, p. 324, doi : 10.1016 / j.compositesb.2006.06.012 .
↑ Regina Valluzzi, Samuel P. Gido, Wayne Muller, David L. Kaplan: Orientation of silk III at the air-water interface. In: International Journal of Biological Macromolecules. 24, 1999, p. 237, doi : 10.1016 / S0141-8130 (99) 00002-1 .
Jump up ↑ Y. Qi, H. Wang, K. Wei, Y. Yang, RY Zheng, IS Kim, KQ Zhang: A Review of Structure Construction of Silk Fibroin Biomaterials from Single Structures to Multi-Level Structures. In: International journal of molecular sciences. Volume 18, number 3, March 2017, p., Doi : 10.3390 / ijms18030237 , PMID 28273799 , PMC 5372488 (free full text).
↑ T. Dyakonov, CH Yang, D. Bush, S. Gosangari, S. Majuru, A. Fatmi: Design and characterization of a silk-fibroin-based drug delivery platform using naproxen as a model drug. In: Journal of drug delivery. Volume 2012, 2012, p. 490514, doi : 10.1155 / 2012/490514 , PMID 22506122 , PMC 3312329 (free full text).

[DOI10.1016/j.compositesb.2006.06.012-1] Osnat Hakimi, David P. Knight, Fritz Vollrath, Pankaj Vadgama: Spider and mulberry silkworm silks as compatible biomaterials. In: Composites Part B: Engineering. 38, 2007, p. 324, doi : 10.1016 / j.compositesb.2006.06.012 .

[DOI10.1016/S0141-8130(99)00002-1-2] Regina Valluzzi, Samuel P. Gido, Wayne Muller, David L. Kaplan: Orientation of silk III at the air-water interface. In: International Journal of Biological Macromolecules. 24, 1999, p. 237, doi : 10.1016 / S0141-8130 (99) 00002-1 .

[3] Jump up ↑ Y. Qi, H. Wang, K. Wei, Y. Yang, RY Zheng, IS Kim, KQ Zhang: A Review of Structure Construction of Silk Fibroin Biomaterials from Single Structures to Multi-Level Structures. In: International journal of molecular sciences. Volume 18, number 3, March 2017, p., Doi : 10.3390 / ijms18030237 , PMID 28273799 , PMC 5372488 (free full text).

[4] T. Dyakonov, CH Yang, D. Bush, S. Gosangari, S. Majuru, A. Fatmi: Design and characterization of a silk-fibroin-based drug delivery platform using naproxen as a model drug. In: Journal of drug delivery. Volume 2012, 2012, p. 490514, doi : 10.1155 / 2012/490514 , PMID 22506122 , PMC 3312329 (free full text).