Fibroin

Last updated
Fibroin light chain
Identifiers
SymbolL-Fibroin
Pfam PF05849
InterPro IPR008660
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary
Fibroin heavy chain
Identifiers
Organism Bombyx mori
SymbolFIBH
PDB 3UA0
UniProt P05790
Search for
Structures Swiss-model
Domains InterPro
For a view of homologs, perform BLAST on the P05790[1-108] portion.
Fibroin P25 (Fibrohexamerin)
Identifiers
SymbolFibroin_P25
Pfam PF07294
InterPro IPR009911
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Fibroin is an insoluble protein present in silk produced by numerous insects, such as the larvae of Bombyx mori , and other moth genera such as Antheraea , Cricula , Samia and Gonometa . Silk in its raw state consists of two main proteins, sericin and fibroin, with a glue-like layer of sericin coating two singular filaments of fibroin called brins. [1] [2] [3] Silk fibroin is considered a β-keratin related to proteins that form hair, skin, nails and connective tissues.

Primary structure of fibroin, (Gly-Ser-Gly-Ala-Gly-Ala)n Silk fibroin primary structure.svg
Primary structure of fibroin, (Gly-Ser-Gly-Ala-Gly-Ala)n

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 of the complex. [4]

The heavy 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. [5] Silk III is formed principally in solutions of fibroin at an interface (i.e. air-water interface, water-oil interface, etc.).

Degradation

Many species of Amycolatopsis and Saccharotrix bacteria are able to degrade both silk fibroin and polylactic acid. [6]

Related Research Articles

<span class="mw-page-title-main">Biopolymer</span> Polymer produced by a living organism

Biopolymers are natural polymers produced by the cells of living organisms. Like other polymers, biopolymers consist of monomeric units that are covalently bonded in chains to form larger molecules. There are three main classes of biopolymers, classified according to the monomers used and the structure of the biopolymer formed: polynucleotides, polypeptides, and polysaccharides. The Polynucleotides, RNA and DNA, are long polymers of nucleotides. Polypeptides include proteins and shorter polymers of amino acids; some major examples include collagen, actin, and fibrin. Polysaccharides are linear or branched chains of sugar carbohydrates; examples include starch, cellulose, and alginate. Other examples of biopolymers include natural rubbers, suberin and lignin, cutin and cutan, melanin, and polyhydroxyalkanoates (PHAs).

<span class="mw-page-title-main">Keratin</span> Structural fibrous protein

Keratin is one of a family of structural fibrous proteins also known as scleroproteins. Alpha-keratin (α-keratin) is a type of keratin found in vertebrates. It is the key structural material making up scales, hair, nails, feathers, horns, claws, hooves, and the outer layer of skin among vertebrates. Keratin also protects epithelial cells from damage or stress. Keratin is extremely insoluble in water and organic solvents. Keratin monomers assemble into bundles to form intermediate filaments, which are tough and form strong unmineralized epidermal appendages found in reptiles, birds, amphibians, and mammals. Excessive keratinization participate in fortification of certain tissues such as in horns of cattle and rhinos, and armadillos' osteoderm. The only other biological matter known to approximate the toughness of keratinized tissue is chitin. Keratin comes in two types, the primitive, softer forms found in all vertebrates and harder, derived forms found only among sauropsids.

<span class="mw-page-title-main">Silk</span> Fine, lustrous, natural fiber produced by various arthropods

Silk is a natural protein fiber, some forms of which can be woven into textiles. The protein fiber of silk is composed mainly of fibroin and is produced by certain insect larvae to form cocoons. The best-known silk is obtained from the cocoons of the larvae of the mulberry silkworm Bombyx mori reared in captivity (sericulture). The shimmering appearance of silk is due to the triangular prism-like structure of the silk fibre, which allows silk cloth to refract incoming light at different angles, thus producing different colors.

<i>Bombyx mori</i> Moth mainly used in the production of silk

Bombyx mori, commonly known as the domestic silk moth, is a moth species belonging to the family Bombycidae. It is the closest relative of Bombyx mandarina, the wild silk moth. Silkworm are the larvae of silk moths. The silkworm is of particular economic value, being a primary producer of silk. The silkworm's preferred food are the leaves of white mulberry, though they may eat other species of mulberry, and even leaves of other plants like the osage orange. Domestic silk moths are entirely dependent on humans for reproduction, as a result of millennia of selective breeding. Wild silk moths, which are other species of Bombyx, are not as commercially viable in the production of silk.

<span class="mw-page-title-main">Spider silk</span> Protein fiber made by spiders

Spider silk is a protein fibre or silk spun by spiders. Spiders use silk to make webs or other structures that function as adhesive traps to catch prey, to entangle and restrain prey before biting, to transmit tactile information, or as nests or cocoons to protect their offspring. They can use the silk to suspend themselves from height, to float through the air, or to glide away from predators. Most spiders vary the thickness and adhesiveness of their silk according to its use.

<span class="mw-page-title-main">Heme</span> Chemical coordination complex of an iron ion chelated to a porphyrin

Heme, or haem, is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver.

<span class="mw-page-title-main">Active site</span> Active region of an enzyme

In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes.

Gonadotropins are glycoprotein hormones secreted by gonadotropic cells of the anterior pituitary of vertebrates. This family includes the mammalian hormones follicle-stimulating hormone (FSH) and luteinizing hormone (LH), the placental/chorionic gonadotropins, human chorionic gonadotropin (hCG) and equine chorionic gonadotropin (eCG), as well as at least two forms of fish gonadotropins. These hormones are central to the complex endocrine system that regulates normal growth, sexual development, and reproductive function. LH and FSH are secreted by the anterior pituitary gland, while hCG and eCG are secreted by the placenta in pregnant humans and mares, respectively. The gonadotropins act on the gonads, controlling gamete and sex hormone production.

<span class="mw-page-title-main">Agitoxin</span>

Agitoxin is a toxin found in the venom of the scorpion Leiurus quinquestriatus hebraeus. Other toxins found in this species include charybdotoxin (CTX). CTX is a close homologue of Agitoxin.

<span class="mw-page-title-main">Protein L</span>

Protein L was first isolated from the surface of bacterial species Peptostreptococcus magnus and was found to bind immunoglobulins through L chain interaction, from which the name was suggested. It consists of 719 amino acid residues. The molecular weight of protein L purified from the cell walls of Peptostreptoccus magnus was first estimated as 95kD by SDS-PAGE in the presence of reducing agent 2-mercaptoethanol, while the molecular weight was determined to 76kD by gel chromatography in the presence of 6 M guanidine HCl. Protein L does not contain any interchain disulfide loops, nor does it consist of disulfide-linked subunits. It is an acidic molecule with a pI of 4.0. Unlike protein A and protein G, which bind to the Fc region of immunoglobulins (antibodies), protein L binds antibodies through light chain interactions. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to protein L.

A nerve guidance conduit is an artificial means of guiding axonal regrowth to facilitate nerve regeneration and is one of several clinical treatments for nerve injuries. When direct suturing of the two stumps of a severed nerve cannot be accomplished without tension, the standard clinical treatment for peripheral nerve injuries is autologous nerve grafting. Due to the limited availability of donor tissue and functional recovery in autologous nerve grafting, neural tissue engineering research has focused on the development of bioartificial nerve guidance conduits as an alternative treatment, especially for large defects. Similar techniques are also being explored for nerve repair in the spinal cord but nerve regeneration in the central nervous system poses a greater challenge because its axons do not regenerate appreciably in their native environment.

<span class="mw-page-title-main">Wild silk</span>

Wild silks have been known and used in many countries from early times, although the scale of production is far smaller than that from cultivated silkworms. Silk cocoons and nests often resemble paper or cloth, and their use has arisen independently in many societies.

Sericin is a protein created by Bombyx mori (silkworms) in the production of silk. Silk is a fibre produced by the silkworm in production of its cocoon. It consists mainly of two proteins, fibroin and sericin. Silk consists of 70–80% fibroin and 20–30% sericin; fibroin being the structural center of the silk, and sericin being the gum coating the fibres and allowing them to stick to each other.

Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:

Demineralizing has the potential to be used in the silk sector enabling wet reeling of Wild Silk moth cocoons by removing the mineral layer present in these cocoons. This technique is not like degumming where the gum of the fibroin fibres is removed what would lead to a tangled cocoon. With "demineralizing" the gum and structure of the cocoon is kept intact enabling the cocoons to be wet reeled. This could allow a new silk industry in areas which have not the conditions or infrastructure for raising the domesticated silk worm Bombyx mori, possibly generating a revolutionary new income stream.

Silk amino acid (SAAs) also known as Sericin is a natural water-soluble glycoprotein extracted from raw silk. It is used as an additive in skin and hair care products due to its high levels of serine which has excellent moisture preservation characteristics. As a water-based additive it is used to provide a protective barrier and silky feel to lotions, soaps, personal lubricants, hair and skincare products. Silk amino acids are produced by hydrolyzing silk proteins into smaller peptide chains, typically 18 to 19 amino acids in length. Silk amino acids have a lower molecular weight than silk protein powders and are moisturizing to skin and hair.

An aquamelt is a naturally hydrated polymeric material that is able to solidify at environmental temperatures through a controlled stress input.

<span class="mw-page-title-main">Protein fold class</span> Categories of protein tertiary structure

In molecular biology, protein fold classes are broad categories of protein tertiary structure topology. They describe groups of proteins that share similar amino acid and secondary structure proportions. Each class contains multiple, independent protein superfamilies.

Caddisfly silk is silk that is secreted by the silk glands of the caddisfly (Trichoptera), similar to Lepidoptera silkworms. The larvae use silk to hunt and defend themselves. The silk's underwater binding properties are a subject of ongoing scientific research.

Tamulotoxin is a venomous neurotoxin from the Indian Red Scorpion.

References

  1. Hakimi O, Knight DP, Vollrath F, Vadgama P (April 2007). "Spider and mulberry silkworm silks as compatible biomaterials". Composites Part B: Engineering. 38 (3): 324–37. doi:10.1016/j.compositesb.2006.06.012.
  2. Dyakonov T, Yang CH, Bush D, Gosangari S, Majuru S, Fatmi A (2012). "Design and characterization of a silk-fibroin-based drug delivery platform using naproxen as a model drug". Journal of Drug Delivery. 2012: 490514. doi: 10.1155/2012/490514 . PMC   3312329 . PMID   22506122.
  3. "Brin definition and meaning | Collins English Dictionary". www.collinsdictionary.com.
  4. Inoue S, Tanaka K, Arisaka F, Kimura S, Ohtomo K, Mizuno S (December 2000). "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". The Journal of Biological Chemistry. 275 (51): 40517–28. doi: 10.1074/jbc.M006897200 . PMID   10986287.
  5. Valluzzi R, Gido SP, Muller W, Kaplan DL (1999). "Orientation of silk III at the air-water interface". International Journal of Biological Macromolecules. 24 (2–3): 237–42. doi:10.1016/S0141-8130(99)00002-1. PMID   10342770.
  6. Tokiwa Y, Calabia BP, Ugwu CU, Aiba S (August 2009). "Biodegradability of plastics". International Journal of Molecular Sciences. 10 (9): 3722–42. doi: 10.3390/ijms10093722 . PMC   2769161 . PMID   19865515.
This article incorporates text from the public domain Pfam and InterPro: IPR009911