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Sericin
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. Structure Sericin is composed of 18 different amino acids, of which 32% is serine. The secondary structure is usually a random coil, but it can also be easily converted into a β-sheet conformation, via repeated moisture absorption and mechanical stretching. The serine hydrogen bonds give its glue-like quality. The genes encoding sericin proteins have been sequenced. Its C-terminal part contains many serine-rich repeats. Using gamma ray examination, it was determined that sericin fibers are composed typically of three layers, all with fibers running in different patterns of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Silk
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. Silk is produced by several insects; but, generally, only the silk of moth caterpillars has been used for textile manufacturing. There has been some research into other types of silk, which differ at the molecular level. Silk is mainly produced by the larvae of insects undergoing complete metamorphosis, but some insects, such as webspinners and raspy crickets, produce silk throughout their lives. Silk production also occurs in hymenoptera ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Silk
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. Silk is produced by several insects; but, generally, only the silk of moth caterpillars has been used for textile manufacturing. There has been some research into other types of silk, which differ at the molecular level. Silk is mainly produced by the larvae of insects undergoing complete metamorphosis, but some insects, such as webspinners and raspy crickets, produce silk throughout their lives. Silk production also occurs in hymenoptera ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Silk Amino Acid
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 (or breaking apart) 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. Silk amino acids are used in formulating shampoos, conditioner, hair treatments, bodywash, body lotions, cleansers, toners and facial moisturizers, mascara, lipstick and color cosmetics. Background Silk is made up of two primary proteins; a fibrous protein known as fibroin, and a sticky protein known as sericin, with t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Fibroin
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. Silk fibroin is considered a β-keratin related to proteins that form hair, skin, nails and connective tissues. 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. 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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Sericulture
Sericulture, or silk farming, is the cultivation of silkworms to produce silk. Although there are several commercial species of silkworms, '' Bombyx mori'' (the caterpillar of the domestic silkmoth) is the most widely used and intensively studied silkworm. Silk was believed to have first been produced in China as early as the Neolithic Period. Sericulture has become an important cottage industry in countries such as Brazil, China, France, India, Italy, Japan, Korea, and Russia. Today, China and India are the two main producers, with more than 60% of the world's annual production. History According to Confucian text, the discovery of silk production dates to about 2700 BC, although archaeological records point to silk cultivation as early as the Yangshao period (5000–3000 BC). In 1977, a piece of ceramic created 5400–5500 years ago and designed to look like a silkworm was discovered in Nancun, Hebei, providing the earliest known evidence of sericulture. Also, by caref ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Keratin
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 saur ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbopol
Poly(acrylic acid) (PAA; trade name Carbomer) is a polymer with the formula (CH2-CHCO2H)n. It is a derivative of acrylic acid (CH2=CHCO2H). In addition to the homopolymers, a variety of copolymers and crosslinked polymers, and partially deprotonated derivatives thereof are known and of commercial value. In a water solution at neutral pH, PAA is an anionic polymer, i.e., many of the side chains of PAA lose their protons and acquire a negative charge. Partially or wholly deprotonated PAAs are polyelectrolytes, with the ability to absorb and retain water and swell to many times their original volume. These properties – acid-base and water-attracting – are the bases of many applications. = Synthesis = PAA is produced by free radical polymerization. Initiators include potassium persulfate and AIBN. Polyacrylic acid is a polyolefin. It can be viewed as polyethylene with carboxylic acid (CO2H) substituents on alternating carbons. Owing to these groups, alternating carbon atom ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pluronic
Poloxamers are nonionic triblock copolymers composed of a central hydrophobic chain of polyoxypropylene (poly(propylene oxide)) flanked by two hydrophilic chains of polyoxyethylene (poly(ethylene oxide)). The word was coined by BASF inventor, Irving Schmolka, who received the patent for these materials in 1973. Poloxamers are also known by the trade names Pluronic, Kolliphor (pharma grade), and Synperonic. Because the lengths of the polymer blocks can be customized, many different poloxamers exist that have slightly different properties. For the generic term ''poloxamer'', these copolymers are commonly named with the letter ''P'' (for poloxamer) followed by three digits: the first two digits multiplied by 100 give the approximate molecular mass of the polyoxypropylene core, and the last digit multiplied by 10 gives the percentage polyoxyethylene content (e.g. P407 = poloxamer with a polyoxypropylene molecular mass of 4000 g/mol and a 70% polyoxyethylene content). For the Pl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Stratum Corneum
The stratum corneum (Latin for 'horny layer') is the outermost layer of the epidermis. The human stratum corneum comprises several levels of flattened corneocytes that are divided into two layers: the ''stratum disjunctum'' and ''stratum compactum''. The skin's protective acid mantle and lipid barrier sit on top of the stratum disjunctum. The stratum disjunctum is the uppermost and loosest layer of skin. The stratum compactum is the comparatively deeper, more compacted and more cohesive part of the stratum corneum. The corneocytes of the stratum disjunctum are larger, more rigid and more hydrophobic than that of the stratum compactum. The stratum corneum is the dead tissue that performs protective and adaptive physiological functions including mechanical shear, impact resistance, water flux and hydration regulation, microbial proliferation and invasion regulation, initiation of inflammation through cytokine activation and dendritic cell activity, and selective permeability to e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hydroxyproline
(2''S'',4''R'')-4-Hydroxyproline, or L-hydroxyproline ( C5 H9 O3 N), is an amino acid, abbreviated as Hyp or O, ''e.g.'', in Protein Data Bank. Structure and discovery In 1902, Hermann Emil Fischer isolated hydroxyproline from hydrolyzed gelatin. In 1905, Hermann Leuchs synthesized a racemic mixture of 4-hydroxyproline. Hydroxyproline differs from proline by the presence of a hydroxyl (OH) group attached to the gamma carbon atom. Production and function Hydroxyproline is produced by hydroxylation of the amino acid proline by the enzyme prolyl hydroxylase following protein synthesis (as a post-translational modification). The enzyme catalyzed reaction takes place in the lumen of the endoplasmic reticulum. Although it is not directly incorporated into proteins, hydroxyproline comprises roughly 4% of all amino acids found in animal tissue, an amount greater than seven other amino acids that are translationally incorporated. Animals Collagen Hydroxyproline is a major ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
