415:
427:
The silk worm produces fibroin with three chains, the light, heavy, and the glycoprotein P25. The heavy and light chains are linked by a disulphide bond, and P25 associates with disulphide-linked heavy and light chains by noncovalent interactions. P25 plays an important role in maintaining integrity
485:
Although silk fibroin has been used for millennia in the textile industry, over the last 20 years, it has become very popular in materials science. This popularity stems from the discovery that silk fibroin (particularly from Bombyx mori) can be redissolved in chaotropic salt solutions such as
476:
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. Silk III is formed principally in solutions of fibroin at an interface (i.e.
461:. 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
486:
calcium chloride or lithium bromide. This process yields an aqueous solution similar to the form found in the silkworm's gland, which can then be used to create various types of materials.
742:
Rizzo, Giorgio; Lo Presti, Marco; Giannini, Cinzia; Sibillano, Teresa; Milella, Antonella; Guidetti, Giulia; Musio, Roberta; Omenetto, Fiorenzo G.; Farinola, Gianluca M. (2021-06-10).
703:
Rizzo, Giorgio; Lo Presti, Marco; Giannini, Cinzia; Sibillano, Teresa; Milella, Antonella; Matzeu, Giusy; Musio, Roberta; Omenetto, Fiorenzo G.; Farinola, Gianluca M. (July 2020).
330:
121:
625:"Silk fibroin of Bombyx mori is secreted, assembling a high molecular mass elementary unit consisting of H-chain, L-chain, and P25, with a 6:6:1 molar ratio"
472:
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
407:
and fibroin, with a glue-like layer of sericin coating two singular filaments of fibroin called brins. Silk fibroin is considered a β-
350:
141:
527:
Hakimi O, Knight DP, Vollrath F, Vadgama P (April 2007). "Spider and mulberry silkworm silks as compatible biomaterials".
170:
665:
872:
338:
129:
556:"Design and characterization of a silk-fibroin-based drug delivery platform using naproxen as a model drug"
387:
334:
125:
705:"Silk Fibroin Processing from CeCl 3 Aqueous Solution: Fibers Regeneration and Doping with Ce(III)"
744:"Bombyx mori Silk Fibroin Regeneration in Solution of Lanthanide Ions: A Systematic Investigation"
502:
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724:
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325:
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116:
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317:
108:
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104:
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82:
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232:
760:
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432:
198:
769:
728:
623:
Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S (December 2000).
381:
17:
838:
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related to proteins that form hair, skin, nails and connective tissues.
854:
819:
399:
286:
203:
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38:
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444:
408:
404:
366:
191:
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136:
31:
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Dyakonov T, Yang CH, Bush D, Gosangari S, Majuru S, Fatmi A (2012).
850:
370:
307:
274:
98:
65:
668:(1999). "Orientation of silk III at the air-water interface".
431:
The heavy fibroin protein consists of layers of antiparallel
606:"Brin definition and meaning | Collins English Dictionary"
418:
Primary structure of fibroin, (Gly-Ser-Gly-Ala-Gly-Ala)
403:. Silk in its raw state consists of two main proteins,
849:
This article incorporates text from the public domain
801:
Tokiwa Y, Calabia BP, Ugwu CU, Aiba S (August 2009).
373:
produced by numerous insects, such as the larvae of
506:bacteria are able to degrade both silk fibroin and
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56:
51:
46:
670:International Journal of Biological Macromolecules
477:air-water interface, water-oil interface, etc.).
748:Frontiers in Bioengineering and Biotechnology
243:For a view of homologs, perform BLAST on the
8:
807:International Journal of Molecular Sciences
298:
210:
89:
828:
818:
777:
759:
640:
581:
571:
413:
519:
252:
152:
43:
7:
709:Macromolecular Chemistry and Physics
629:The Journal of Biological Chemistry
25:
541:10.1016/j.compositesb.2006.06.012
439:mainly consists of the recurrent
27:Insoluble protein present in silk
379:, and other moth genera such as
664:Valluzzi R, Gido SP, Muller W,
803:"Biodegradability of plastics"
529:Composites Part B: Engineering
1:
682:10.1016/S0141-8130(99)00002-1
302:Available protein structures:
93:Available protein structures:
37:For spider silk protein, see
256:Fibroin P25 (Fibrohexamerin)
894:
848:
36:
29:
761:10.3389/fbioe.2021.653033
610:www.collinsdictionary.com
297:
242:
209:
88:
560:Journal of Drug Delivery
30:Not to be confused with
721:10.1002/macp.202000066
642:10.1074/jbc.M006897200
424:
417:
820:10.3390/ijms10093722
573:10.1155/2012/490514
156:Fibroin heavy chain
47:Fibroin light chain
425:
481:Materials science
437:primary structure
360:
359:
356:
355:
351:structure summary
251:
250:
238:
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142:structure summary
16:(Redirected from
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635:(51): 40517–28.
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494:Many species of
428:of the complex.
365:is an insoluble
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90:
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873:Insect proteins
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676:(2–3): 237–42.
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508:polylactic acid
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28:
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15:
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5:
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813:(9): 3722–42.
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535:(3): 324–37.
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497:Amycolatopsis
489:
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469:manufacture.
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503:Saccharotrix
501:
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18:Silk fibroin
490:Degradation
474:Bombyx mori
463:biomedicine
433:beta sheets
376:Bombyx mori
369:present in
269:Fibroin_P25
261:Identifiers
223:Swiss-model
171:Bombyx mori
161:Identifiers
52:Identifiers
867:Categories
566:: 490514.
514:References
443:sequence (
441:amino acid
314:structures
219:Structures
214:Search for
105:structures
859:IPR009911
770:2296-4185
729:1022-1352
666:Kaplan DL
455:-Gly-Ala)
382:Antheraea
292:IPR009911
83:IPR008660
60:L-Fibroin
855:InterPro
839:19865515
788:34178956
690:10342770
651:10986287
592:22506122
400:Gonometa
331:RCSB PDB
287:InterPro
247:portion.
233:InterPro
166:Organism
122:RCSB PDB
78:InterPro
39:Spidroin
830:2769161
779:8222627
583:3312329
467:textile
409:keratin
405:sericin
388:Cricula
367:protein
363:Fibroin
280:PF07294
229:Domains
199:UniProt
71:PF05849
837:
827:
786:
776:
768:
727:
715:(13).
688:
649:
590:
580:
435:. Its
346:PDBsum
320:
310:
266:Symbol
245:P05790
204:P05790
178:Symbol
137:PDBsum
111:
101:
57:Symbol
32:Fibrin
451:-Gly-
394:Samia
878:Silk
853:and
851:Pfam
835:PMID
784:PMID
766:ISSN
725:ISSN
686:PMID
647:PMID
588:PMID
564:2012
500:and
465:and
397:and
371:silk
339:PDBj
335:PDBe
318:ECOD
308:Pfam
275:Pfam
192:3UA0
181:FIBH
130:PDBj
126:PDBe
109:ECOD
99:Pfam
66:Pfam
825:PMC
815:doi
774:PMC
756:doi
717:doi
713:221
678:doi
637:doi
633:275
578:PMC
568:doi
537:doi
453:Ala
449:Ser
445:Gly
326:PDB
187:PDB
117:PDB
869::
857::
833:.
823:.
811:10
809:.
805:.
782:.
772:.
764:.
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750:.
746:.
723:.
711:.
707:.
684:.
674:24
672:.
645:.
631:.
627:.
608:.
586:.
576:.
562:.
558:.
533:38
531:.
510:.
391:,
385:,
337:;
333:;
316:/
128:;
124:;
107:/
841:.
817::
790:.
758::
752:9
731:.
719::
692:.
680::
653:.
639::
612:.
594:.
570::
543:.
539::
458:n
447:-
421:n
41:.
34:.
20:)
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