Bioretin омолаживающий крем

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Bioretin Омолаживающий Крем

IUPAC name

5-[(3aS,4S,6aR)oxohexahydro-1H-thieno[3,4-d]imidazolyl]pentanoic acid

Other names

Vitamin B7; Vitamin H; Coenzyme R; Biopeiderm


CAS Number

3D model (JSmol)

ECHA InfoCard






  • InChI=1S/C10H16N2O3S/c(14)()(15)/h,9H,H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1&#;Y
  • InChI=1/C10H16N2O3S/c(14)()(15)/h,9H,H2,(H,13,14)(H2,11,12,15)/t6-,7-,9-/m0/s1




Chemical formula

Molar mass&#;g·mol−1
AppearanceWhite crystalline needles
Melting point to &#;°C ( to &#;°F; to &#;K)

Solubility in water

22 mg/ mL

ATC code

A11HA05 (WHO)

Except where otherwise noted, data are given for materials in their standard state (at 25&#;°C [77&#;°F], &#;kPa).

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Biotin is a water-soluble B vitamin,[2] also called vitamin B7 and formerly known as vitamin H or coenzyme R.[3]

It is composed of a ureido ring fused with a tetrahydrothiophene ring.

A valeric acid substituent is attached to one of the carbon atoms of the tetrahydrothiophene ring. Biotin is a coenzyme for carboxylase enzymes, involved in the synthesis of fatty acids, isoleucine, and valine, and in gluconeogenesis.[3]

Biotin deficiency can be caused by inadequate dietary intake or inheritance of one or more inborn genetic disorders that affect biotin metabolism.[2][3] Subclinical deficiency can cause mild symptoms, such as hair thinning or skin rash typically on the face.[2] Neonatal screening for biotinidase deficiency began in the United States inwith many countries testing for this disorder at birth.

Individuals born prior to are unlikely to have been screened, obscuring the true prevalence of the disorder.[2]


Biotin is an important component of enzymes involved in metabolizing fats and carbohydrates, influencing cell growth, and affecting amino acids involved in protein synthesis.[2][3] Biotin assists in various metabolic reactions involving the transfer of carbon dioxide. It may also be helpful in maintaining a steady blood sugar level.

Biotin is often recommended as a dietary supplement for strengthening hair and nails, though scientific data supporting these outcomes are weak.[3] Nevertheless, biotin is found in many cosmetics and health products for the hair and skin.[4][5]

Biotin deficiency is rare.[2] The amounts needed are small, a wide range of foods contain biotin, and intestinal bacteria synthesize biotin, which is then absorbed by the host animal.

For that reason, statutory agencies in many countries, for example the USA[6] and Australia,[7] have not formally established a recommended daily intake of biotin. Instead, an Adequate Intake (AI) is identified based on the theory that average intake meets needs. Future research could result in biotin AIs with EARs and RDAs (see Dietary Reference Intake section).

A number of rare metabolic disorders exist in which an individual's metabolism of biotin is abnormal, such as deficiency in the holocarboxylase synthetase enzyme which covalently links biotin onto the carboxylase, where the biotin acts as a cofactor.[8]


Biotin has an unusual structure (above figure), with two rings fused together via one of their sides.

The two rings are ureido and thiophene moieties. Biotin is a heterocyclic, S-containing monocarboxylic acid. It is made from two precursors, alanine and pimeloyl-CoA via three enzymes.

8-Aminooxopelargonic acid synthase is a pyridoxal 5'-phosphate enzyme. The pimeloyl-CoA, could be produced by a modified fatty acid pathway involving a malonyl thioester as the starter. 7,8Diaminopelargonic acid (DAPA) aminotransferase is unusual in using S-adenosyl methionine (SAM) as the NH2 donor. Dethiobiotin synthetase catalyzes the formation of the ureido ring via a DAPA carbamate activated with ATP. Biotin synthase reductively cleaves SAM into a deoxyadenosyl radical, which abstracts an H atom from dethiobiotin to give an intermediate that is trapped by the sulfur donor.

This sulfur donor is an iron-sulfur cluster.[9]

Cofactor biochemistry[edit]

D-(+)-Biotin is a cofactor responsible for carbon dioxide transfer in several carboxylaseenzymes:

Biotin is important in fatty acid synthesis, branched-chain amino acid catabolism, and gluconeogenesis.[2][3] It covalently attaches to the epsilon-amino group of specific lysine residues in these carboxylases.

This biotinylation reaction requires ATP and is catalyzed by holocarboxylase synthetase.[10] In bacteria, biotin is attached to biotin carboxyl carrier protein (BCCP) by biotin protein ligase (BirA in E.

coli).[11] The attachment of biotin to various molecules, biotinylation, is used as an important laboratory technique to study various processes, including protein localization, protein interactions, DNAtranscription, and replication. Biotinidase itself is known to be able to biotinylate histone proteins,[12] but little biotin is found naturally attached to chromatin.

Biotin binds tightly to the tetrameric protein avidin (also streptavidin and neutravidin), with a dissociation constantKd on the order of 10−15 M, which is one of the strongest known protein-ligand interactions.[13] This is often used in different biotechnological applications.

Untilvery harsh conditions were thought to be required to break the biotin-streptavidin interaction.[14]

Dietary recommendations[edit]

The U.S. Institute of Medicine updated Estimated Average Requirements (EARs) and Recommended Dietary Allowances (RDAs) for biotin in [2][15] At that time, there was insufficient information to establish EARs and RDAs for biotin.

In instances such as this, the Board sets Adequate Intakes (AIs) with the understanding that, at some later date when the physiological effects of biotin are better understood, AIs will be replaced by more exact information.

The AIs for biotin are: 5mcg of biotin for month-old males, 6mcg of biotin for month-old males, 8mcg of biotin for year-old males, 12mcg of biotin for year-old males, 20mcg of biotin for year-old males, 25mcg of biotin for year-old males, and 30mcg of biotin for males that are 19 years old and older.

The AIs for biotin are: 5mcg of biotin for month-old females, 6mcg of biotin for month-old females, 8mcg of biotin for year-old females, 12mcg of biotin for year-old females, 20mcg of biotin for year-old females, 25mcg of biotin for year-old females, and 30mcg of biotin for females that are 19 years old and older.

The AIs for biotin are: 0mcg of biotin for year-old pregnant females; furthermore, 35mcg of biotin for year-old lactating females.[2][3][15] As for safety, the Institute of Medicine estimates Tolerable Upper Intake Levels (known as ULs) for vitamins and minerals when evidence for a true upper limit is sufficient.

For biotin, however, there is no UL because adverse effects of high biotin intake have not been determined. Collectively the EARs, RDAs, AIs and ULs are referred to as Dietary Reference Intakes (DRIs).[15]

The European Food Safety Authority (EFSA) refers to the collective set of information as Dietary Reference Values, with Population Reference Intake instead of RDA, and Average Requirement instead of EAR.

AI and UL are defined the same as in United States. For women and men over age 18, the Adequate Intake is set at 40 μg per day. The AI for pregnancy is 40 μg per day, and 45 μg per day during breastfeeding. For children ages 1–17 years, the AIs increase with age from 20 to 35 μg per day.[16] EFSA also reviewed safety and reached the same conclusion as in United States that there is insufficient evidence to set a Tolerable Upper Limit for biotin.[17]

For the United States food and dietary supplement labeling purposes, the amount in a serving is expressed as a percent of Daily Value (DV).

For biotin labeling purposes, % of the Daily Value was revised in to 30 μg per day to bring it into agreement with the AI.[18] The original deadline to be in compliance was July 28,but on September 29,the FDA released a proposed rule that extended the deadline to January 1, for large companies and January 1, for small companies to make changes in product labeling.[19]


Biotin is synthesized by intestinalbacteria, but there is a lack of good quality studies about how much biotin they provide.[3]

Biotin is stable at room temperature and is not destroyed by cooking.

Sources with appreciable content are:[2][3]

  • Beef or pork liver, cooked: up to 35 μg per 3 ounce serving
  • Egg, cooked: up to 25 μg per large egg
  • Yeast, baker's, dried: up to 14 μg per 7 gram packet
  • Whole wheat bread: up to 6 μg per slice
  • Avocado: up to 6 μg per avocado
  • Salmon, cooked: up to 5 μg per 3 ounce serving
  • Cauliflower, raw: up to 4 μg per cup
  • Cheese, cheddar: up to 2 μg per ounce

Raw egg whites contain a protein (avidin) that blocks the absorption of biotin, so people who regularly consume a large number of raw eggs may become biotin-deficient.[15] The dietary biotin intake in Western populations has been estimated to be as high as 60 μg per day.[3] Biotin is also available in dietary supplements,[2] individually or as an ingredient in multivitamins.[3]


Biotin is also called vitamin H (the H represents Haar und Haut, German words for "hair and skin") or vitamin B7.

Studies on its bioavailability have been conducted in rats and in chicks. Based on these studies, biotin bioavailability may be low or variable, depending on the type of food being consumed. In general, biotin exists in food as protein-bound form or biocytin.[20] Proteolysis by protease is required prior to absorption. This process assists free biotin release from biocytin and protein-bound biotin.

The biotin present in corn is readily available; however, most grains have about a % bioavailability of biotin.[21]

The wide variability in biotin bioavailability may be due to the ability of an organism to break various biotin-protein bonds from food.

Whether an organism has an enzyme with that ability will determine the bioavailability of biotin from the foodstuff.[21]

Factors that affect biotin requirements[edit]

The frequency of marginal biotin status is not known, but the incidence of low circulating biotin levels in alcoholics has been found to be much greater than in the general population.

Also, relatively low levels of biotin have been reported in the urine or plasma of patients who have had a partial gastrectomy or have other causes of achlorhydria, burn patients, epileptics, elderly individuals, and athletes.[21] Pregnancy and lactation may be associated with an increased demand for biotin.

In pregnancy, this may be due to a possible acceleration of biotin catabolism, whereas, in lactation, the higher demand has yet to be elucidated. Recent studies have shown marginal biotin deficiency can be present in human gestation, as evidenced by increased urinary excretion of 3-hydroxyisovaleric acid, decreased urinary excretion of biotin and bisnorbiotin, and decreased plasma concentration of biotin. Additionally, smoking may further accelerate biotin catabolism in women.[22]


Biotin deficiency typically occurs from absence of the vitamin in the diet, particularly in breastfeeding mothers.[2] Daily consumption of raw egg whites for several months may result in biotin deficiency[23], due to their avidin content.

Deficiency can be addressed with nutritional supplementation.[23]

Deficiency symptoms include:[2]

  • Brittle and thin fingernails
  • Hair loss (alopecia)
  • Conjunctivitis
  • Dermatitis in the form of a scaly, red rash around the eyes, nose, mouth, and genital area.
  • Neurological symptoms in adults, such as depression, lethargy, hallucination, and numbness and tingling of the extremities[23]

The neurological and psychological symptoms can occur with only mild deficiencies.

Dermatitis, conjunctivitis, and hair loss will generally occur only when deficiency becomes more severe.[23] Individuals with hereditary disorders of biotin deficiency have evidence of impaired immune system function, including increased susceptibility to bacterial and fungal infections.[3] Pregnant women tend to have a higher risk of biotin deficiency. Nearly half of pregnant women have abnormal increases of 3-hydroxyisovaleric acid, which reflects reduced status of biotin.[3]

Metabolic disorders[edit]

Inherited metabolic disorders characterized by deficient activities of biotin-dependent carboxylases are termed multiple carboxylase deficiency.

These include deficiencies in the enzymes holocarboxylase synthetase or biotinidase.[2]Holocarboxylase synthetase deficiency prevents the body's cells from using biotin effectively, and thus interferes with multiple carboxylase reactions.[24] Biochemical and clinical manifestations include: ketolactic acidosis, organic aciduria, hyperammonemia, skin rash, feeding problems, hypotonia, seizures, developmental delay, alopecia, and coma.

Biotinidase deficiency is not due to inadequate biotin, but rather to a deficiency in the enzymes that process it.[2]Biotinidase catalyzes the cleavage of biotin from biocytin and biotinyl-peptides (the proteolytic degradation products of each holocarboxylase) and thereby recycles biotin.

It is also important in freeing biotin from dietary protein-bound biotin.[24] General symptoms include decreased appetite and growth. Dermatologic symptoms include dermatitis, alopecia, and achromotrichia (absence or loss of pigment in the hair). Perosis (a shortening and thickening of bones) is seen in the skeleton.

Fatty liver and kidney syndrome and hepatic steatosis also can occur.[21]

Use in biotechnology[edit]

Biotin is widely used throughout the biotechnology industry to conjugate proteins for biochemical assays.[25] Biotin's small size means the biological activity of the protein will most likely be unaffected. This process is called biotinylation. Because both streptavidin and avidin bind biotin with high affinity (Kd of 10−14&#;mol/l to 10−15&#;mol/l) and specificity, biotinylated proteins of interest can be isolated from a sample by exploiting this highly stable interaction.

The sample is incubated with streptavidin/avidin beads, allowing capture of the biotinylated protein of interest. Any other proteins binding to the biotinylated molecule will also stay with the bead and all other unbound proteins can be washed away.

However, due to the extremely strong streptavidin-biotin interaction, very harsh conditions are needed to elute the biotinylated protein from the beads (typically 6M guanidine HCl at pH&#;), which often will denature the protein of interest. To circumvent this problem, beads conjugated to monomeric avidin can be used, which has a decreased biotin-binding affinity of ~10−8&#;mol/l, allowing the biotinylated protein of interest to be eluted with excess free biotin.

As one of the strongest non-covalent interactions, the binding of biotin to streptavidin is commonly used as the target molecular interaction in the research of biosensors and cell sorting.[26][27]

ELISAs often make use of biotinylated detection antibodies against the antigen of interest, followed by a detection step using streptavidin conjugated to a reporter molecule, such as horseradish peroxidase or alkaline phosphatase.

Medical laboratory testing[edit]

Biotin in samples taken from people ingesting high levels of biotin in dietary supplements may affect diagnostic test results.[2][28]


Because there are no reported cases of adverse effects from receiving high doses of biotin, there are no tolerable upper intake levels established in the United States.[2][3]

See also[edit]


  1. ^Merck Index, 11th Edition, .
  2. ^ abcdefghijklmnopq"Biotin – Fact Sheet for Health Professionals".

    Office of Dietary Supplements, US National Institutes of Health. 8 December Retrieved 25 February &#;

  3. ^ abcdefghijklmn"Biotin".

    Micronutrient Information Center, Linus Pauling Institute, Oregon State University, Corvallis, OR. 21 October Retrieved 16 January &#;

  4. ^"Final report on the safety assessment of biotin". Int J Toxicol. 20 Suppl 4: 1– PMID&#;&#;
  5. ^"Vitamin H (Biotin)". University of Maryland Medical Center.

    1 June Retrieved 4 May &#;

  6. ^Otten, JJ; Hellwig, JP; Meyers, LD., eds. (). Dietary Reference Intakes: The Essential Guide to Nutrient Requirements. The National Academies Press. ISBN&#;&#;
  7. ^National Health and Medical Research Council: Nutrient Reference Values for Australia and New Zealand
  8. ^Zempleni J, Hassan YI, Wijeratne SS ().

    "Biotin and biotinidase deficiency". Expert Rev Endocrinol Metab. 3 (6): – doi/ PMC&#;. PMID&#;&#;

  9. ^Marquet A, Bui BT, Florentin D (). "Biosynthesis of biotin and lipoic acid". Vitam. Horm. Vitamins & Hormones. 61: 51– doi/S(01) ISBN&#; PMID&#;&#;
  10. ^Zempleni J, Wijeratne SS, Hassan YI (). "Biotin". BioFactors.

    35 (1): 36– doi/biof PMC&#;. PMID&#;&#;

  11. ^Chapman-Smith A, Cronan JE (). "Molecular biology of biotin attachment to proteins". J. Nutr. (2S Suppl): S–S. PMID&#;&#;
  12. ^Hymes J, Fleischhauer K, Wolf B (). "Biotinylation of histones by human serum biotinidase: assessment of biotinyl-transferase activity in sera from normal individuals and children with biotinidase deficiency".

    Biochem Mol Med. 56 (1): 76– doi/bmme PMID&#;&#;

  13. ^Laitinen OH, Hytönen VP, Nordlund HR, Kulomaa MS (). "Genetically engineered avidins and streptavidins". Cell Mol Life Sci. 63 (24): – doi/sz. PMID&#;&#;
  14. ^Holmberg A, Blomstergren A, Nord O, Lukacs M, Lundeberg J, Uhlén M ().

    "The biotin-streptavidin interaction can be reversibly broken using water at elevated temperatures". Electrophoresis. 26 (3): – doi/elps PMID&#;&#;

  15. ^ abcdInstitute of Medicine (). "Biotin". Dietary Reference Intakes for Thiamin, Riboflavin, Niacin, Vitamin B6, Folate, Vitamin B12, Pantothenic Acid, Biotin, and Choline.

    Washington, DC: The National Academies Press. pp.&#;– ISBN&#; Retrieved &#;

  16. ^"Overview on Dietary Reference Values for the EU population as derived by the EFSA Panel on Dietetic Products, Nutrition and Allergies"(PDF).


  17. ^"Tolerable Upper Intake Levels For Vitamins And Minerals"(PDF). European Food Safety Authority. &#;
  18. ^"Federal Register May 27, Food Labeling: Revision of the Nutrition and Supplement Facts Labels"(PDF).&#;
  19. ^"Changes to the Nutrition Facts Panel - Compliance Date"
  20. ^Gropper SS, Smith JL, Groff JL ().

    Advanced nutrition and human metabolism. Belmont. ISBN&#;&#;

  21. ^ abcdCombs, Gerald F. Jr. (). The Vitamins: Fundamental Aspects in Nutrition and Health. San Diego: Elsevier, Inc. ISBN&#;&#;
  22. ^Bowman, BA; Russell, RM., eds. (). "Biotin". Present Knowledge in Nutrition, Ninth Edition, Vol 1. Washington, DC: International Life Sciences Institute.


  23. ^ abcd"Biotin: MedlinePlus Supplements". 13 September Retrieved &#;
  24. ^ abWolf B, Grier RE, Secor McVoy JR, Heard GS ().

    "Biotinidase deficiency: a novel vitamin recycling defect". J Inherit Metab Dis. 8 (1): 53–8. doi/BF PMID&#;&#;

  25. ^"Overview of Protein Labeling". Thermo Fisher Scientific. Retrieved 22 April &#;
  26. ^Xu, Zhida; Xinhao, Wang; Han, Kevin; Li, Shuo; Liu, Logan (). "Elastomeric 2D grating and hemispherical optofluidic chamber for multifunctional fluidic sensing". Journal of the Optical Society of America A.

    30 (12). pp. – arXiv. doi/JOSAA&#;

  27. ^Xu, Zhida; Jiang, Jing; Wang, Xinhao; Han, Kevin; Ameen, Abid; Khan, Ibrahim; Chang, Te-Wei; Liu, Logan (). "Large-area, uniform and low-cost dual-mode plasmonic naked-eye colorimetry and SERS sensor with handheld Raman spectrometer".

    Nanoscale. 8 (11): – arXiv. doi/C5NRE.&#;

  28. ^"The FDA Warns that Biotin May Interfere with Lab Tests: FDA Safety Communication". US Food and Drug Administration. 28 November Retrieved 11 December &#;
Dean Burk, American biochemist working on isolation of biotin.

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