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Biotin
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In one pass Biotin (B7) is the vitamin that supplement marketing sells for hair, nails, and skin.
Educational content, not medical advice — consult a clinician.
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Chapter 1
Helps four enzymes add a carbon
Biotin (B7) is the vitamin that supplement marketing sells for hair, nails, and skin. Its real job in the body has little direct link to hair: it is the shared key for four key metabolic enzymes, and it sits on three production lines at once, for sugar, fat, and amino acids.
All four locks are carboxylases, enzymes that do the same kind of work: they attach one carbon (a carboxyl group) to a molecule. Biotin is bound firmly to each enzyme, and without it all four machines stop. Each has its own stretch. During fasting, liver cells attach a carbon to pyruvate and turn it into oxaloacetate, the starting point for the liver making its own glucose (gluconeogenesis). On the fat-making line, acetyl-CoA takes on a carbon to become malonyl-CoA, the step where building a fatty acid begins. The other two locks take leucine and odd-chain fatty acids apart and feed them into the energy-producing cycle. One vitamin sits on three main roads at once, which is why it is so basic.
Its real-world risk is not shortage but excess: a few milligrams a day or more can distort many lab results, so stop it before a blood test and tell the doctor.
All four locks are carboxylases, enzymes that do the same kind of work: they attach one carbon (a carboxyl group) to a molecule. Biotin is bound firmly to each enzyme, and without it all four machines stop. Each has its own stretch. During fasting, liver cells attach a carbon to pyruvate and turn it into oxaloacetate, the starting point for the liver making its own glucose (gluconeogenesis). On the fat-making line, acetyl-CoA takes on a carbon to become malonyl-CoA, the step where building a fatty acid begins. The other two locks take leucine and odd-chain fatty acids apart and feed them into the energy-producing cycle. One vitamin sits on three main roads at once, which is why it is so basic.
Its real-world risk is not shortage but excess: a few milligrams a day or more can distort many lab results, so stop it before a blood test and tell the doctor.
Mechanism · What goes into and out of each lock
Each of the four locks has its own stretch of work. Below, the four chains are walked one by one, each as what goes in, what comes out, and therefore what the body can do.The first lock · pyruvate carboxylase
The feedstock is pyruvate, the part left over once glucose has been taken halfway apart. This lock sits in the mitochondria of liver cells. It attaches one carbon to pyruvate, and the output is oxaloacetate.
Oxaloacetate is the first brick of gluconeogenesis, a reverse assembly line: starting from it, the liver builds backward, reassembling lactate, glycerol, and glucogenic amino acids into glucose, then sends that glucose into the blood for the brain and red blood cells, the tissues that depend on glucose the most. So the answer to what holds blood glucose up after a night without food lands on this step. Without biotin, pyruvate cannot take on that carbon, and nobody lays the first brick of the return trip.
Oxaloacetate has a second identity: it is the entry molecule of the citric acid cycle, and every turn of the cycle needs it to catch acetyl-CoA. So when this lock slows down, the cycle that burns fat for energy turns poorly too.
The second lock · acetyl-CoA carboxylase (ACC)
The feedstock is acetyl-CoA, the two-carbon part that both sugar and fat become when taken all the way apart. Attach one carbon and the output is malonyl-CoA. This is the first step in building fatty acids from scratch, and it is the checkpoint on the whole line that decides whether work starts at all.
Once made, malonyl-CoA has a second job, and it is the part most worth remembering: it blocks the transport protein at the mitochondrial door that carries long-chain fatty acids inside (carnitine palmitoyltransferase 1, CPT1). Fatty acids can only be broken down for energy once they are inside the mitochondria, so at the same moment the body is making fat, it also narrows the door for burning fat, instead of making and burning at once and spinning in place. After a meal the switch leans toward making; when you are hungry it leans toward burning; and what flips it is this lock's product.
The third lock · the one that breaks down leucine (MCC, methylcrotonyl-CoA carboxylase)
Leucine is the best-known branched-chain amino acid. Partway through its breakdown it reaches a junction where a carbon must be attached before it can go on, and MCC stands at that junction.
When this chain backs up, the half-broken-down leucine intermediate piles up and is diverted out in the urine as 3-hydroxyisovaleric acid. The urine marker used to judge whether pregnant women have enough biotin leaks from exactly this junction. That explains something counterintuitive: when the body starts running short of biotin, the first thing a test picks up is often not a fall in blood biotin but a rise in this urine marker.
The fourth lock · propionyl-CoA carboxylase (PCC)
The feedstock is propionyl-CoA, which has two sources: the leftover three-carbon tail once odd-chain fatty acids are taken apart, and the breakdown products of some branched-chain amino acids. PCC attaches one carbon so it can join the citric acid cycle and produce energy. Without this step, these leftovers stall halfway; they cannot be burned and are hard to clear.
Putting the four locks back on one map
Pyruvate carboxylase handles making sugar. ACC handles making fat, and along the way regulating fat burning. MCC and PCC handle feeding amino-acid and fatty-acid leftovers back onto the main road. Each of the three main roads, sugar, fat, and amino acids, has a junction that needs a carbon attached before traffic can pass, and all four junctions use the same key. People with severe biotin deficiency show symptoms in skin, hair, and nerves at the same time; one explanation is that no single organ has failed, but all three metabolic main roads have slowed down together.
Myth · Does biotin make your hair thicker?
"Biotin makes hair and nails thicker and fuller" is one of the biggest traffic drivers in the supplement market. Here is the evidence, point by point.The real part: severe biotin deficiency does cause hair loss, skin rash, and brittle nails. This was seen in 1940s experiments in which volunteers ate large amounts of raw egg white, and in a rare inherited disease (biotinidase deficiency); once the deficiency is corrected, hair and nails recover. For brittle nails, a few small studies such as Hochman 1993 and Colombo 1990 gave high-dose biotin (2.5 mg/day for 6–15 months) and saw the nails improve. None had a placebo group, Hochman 1993 was a retrospective review of past patient records, and none measured whether the participants lacked biotin to begin with. No large has reproduced the result.
The over-extended part: there is no randomized controlled trial showing that healthy people who are not short of biotin get thicker, denser hair by taking it. The Patel 2017 review (published in Skin Appendage Disorders) searched the literature and found only 18 case reports, not a single randomized controlled trial, and every one of those 18 patients had an underlying condition that was stopping their hair or nails from growing well. Biotin helping them shows that correcting a disease state works, not that healthy people do better. The Soleymani 2017 review likewise noted that no clinical trial has ever studied biotin for any kind of hair loss, so it is not routinely recommended.
The misconception persists for a few reasons. Hair and nails grow slowly (hair about 1 cm a month, nails about 3 mm a month), so any 3–6 months of supplementation comes with visible new growth, which feels like it worked. Hair problems have many causes (stress, sleep, hormones, iron, thyroid, androgenetic alopecia), and a natural recovery while taking biotin is easily credited to the biotin. And it is cheap, nearly free of side effects, and reassuring, which makes it very profitable.
What is actually worth checking first is a different set of factors:
Enough protein (hair is mostly keratin, and hair thins first when protein runs short)Enough iron: low (a measure of the body's iron stores) is the first thing to check in women's hair lossNormal thyroid function (whether and related tests fall within the reference range)Enough vitamin D ( ≥ 20 ng/mL, that is, 50 nmol/L)Enough zinc and seleniumSleep and stress: about 3 months after an acute stress or a serious illness, a temporary shedding called telogen effluvium can appearHormonal status in women (polycystic ovary syndrome, perimenopause), with an endocrine workup if neededMale androgenetic alopecia: minoxidil and finasteride are backed by several randomized trials; these are the real drugs
In 2017 the FDA also issued a safety communication about biotin: high-dose biotin (> 5 mg/day) interferes with immunoassays, especially troponin, the test used to diagnose a heart attack, making results falsely low. The FDA received a report of a patient on high-dose biotin whose troponin read falsely low and who later died. Biotin also interferes with thyroid tests (TSH, ) and sex-hormone tests, producing a picture that looks like hyperthyroidism. The clinical advice is to stop biotin at least 48 hours before a blood test and to tell your doctor.
In practice: healthy hair and nails rest on overall nutrition plus finding the real cause, not on biotin alone. If you already take it, it is not really a safety problem (apart from the lab interference), but do not expect results unless a deficiency has been found.
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Chapter 2
Food and gut sources
Biotin is widespread in food, and the richest sources are organ meats, eggs, fish, and meat:
High: beef liver (about 27 µg per 75 g), one cooked egg (about 10 µg, mostly in the yolk), a serving of canned salmon (about 5 µg)
Lower: plant foods such as sweet potato, almonds, spinach, and broccoli
Fortified foods: many breakfast cereals are fortified
Gut bacteria also make biotin, but how much they actually contribute to the body is hard to pin down: everyone's microbiome is different, and how well the colon absorbs biotin is uncertain.
The adult adequate intake () is 30 µg/day (the data are too thin to set a recommended amount, an , so an AI is used). An ordinary varied diet usually covers it; severe biotin deficiency has never been reported in healthy people eating a normal mixed diet.
High: beef liver (about 27 µg per 75 g), one cooked egg (about 10 µg, mostly in the yolk), a serving of canned salmon (about 5 µg)
Lower: plant foods such as sweet potato, almonds, spinach, and broccoli
Fortified foods: many breakfast cereals are fortified
Gut bacteria also make biotin, but how much they actually contribute to the body is hard to pin down: everyone's microbiome is different, and how well the colon absorbs biotin is uncertain.
The adult adequate intake () is 30 µg/day (the data are too thin to set a recommended amount, an , so an AI is used). An ordinary varied diet usually covers it; severe biotin deficiency has never been reported in healthy people eating a normal mixed diet.
Numbers · How much comes from gut vs food
"Gut bacteria produce biotin" is a common claim. More precisely: they do produce it, but how much they contribute is uncertain.What is known: several kinds of gut bacteria (some members of the Bacteroidetes, Firmicutes, and Proteobacteria) can make biotin, mostly in the colon, and the cells lining the colon carry a sodium-dependent multivitamin transporter (SMVT) that can absorb it.
What is still debated: estimates of how much gut bacteria actually add to the body's biotin range from 5% to 50% (the Said 2009 review), with huge differences between people. It is hard to study on its own, because people cannot be made completely free of gut bacteria. Some observations suggest that biotin status usually changes little after antibiotics, an indirect sign that food is still the main source.
A shortfall in the bacterial share shows up only in a few special situations: people on long-term broad-spectrum antibiotics who also eat poorly and depend on intravenous feeding (TPN) may see their biotin status fall, and so may some patients with severe disruption of the gut bacteria (such as Clostridioides difficile infection, CDI, or inflammatory bowel disease, ). None of these are situations an ordinary person needs to worry about.
Reference biotin content of common foods (mostly from the food table of the US NIH Office of Dietary Supplements):
Cooked egg: about 10 µg each (mostly in the yolk)Beef liver: about 27 µg per 75 gCanned salmon: about 5 µg per servingBroccoli: about 0.4 µg per half cupAlmonds: about 1.5 µg per 22 nutsNutritional yeast: about 2 µg per tablespoonSweet potato: about 2.4 µg per half cup
The adult is 30 µg/day, which 2 eggs plus some vegetables and nuts a day will basically reach.
Cooking losses are small too: the biotin in eggs is fairly heat-stable, and cooked yolk holds about as much as raw yolk. Raw egg white contains avidin, a protein that locks up biotin, which is one more reason cooked eggs are the better choice. Long stewing loses less than 20%, and baking loses less than 10%.
Chapter 3
Raw egg white traps biotin
Raw egg white contains a protein called avidin that binds biotin extremely tightly (a dissociation constant, Kd, of about 10⁻¹⁵ mol/L), one of the strongest non-covalent protein-ligand bonds known. Once avidin has caught biotin, the gut cannot absorb it.
Heat inactivates avidin: when egg white is cooked, this protein unfolds and stops grabbing biotin, so ordinary boiled or scrambled eggs cause no problem at all.
The real risk: eating large amounts of raw egg white for a long time (some people in fitness circles do) can cause biotin deficiency, and there are case reports. Cooking the egg solves it completely. It is not a reason to skip the yolk; it is a reminder not to eat lots of raw egg white for months on end.
Streptavidin, a common laboratory protein, is a structural relative of avidin, and the biotin-streptavidin pair is one of the most widely used molecular tagging systems in biotechnology.
Heat inactivates avidin: when egg white is cooked, this protein unfolds and stops grabbing biotin, so ordinary boiled or scrambled eggs cause no problem at all.
The real risk: eating large amounts of raw egg white for a long time (some people in fitness circles do) can cause biotin deficiency, and there are case reports. Cooking the egg solves it completely. It is not a reason to skip the yolk; it is a reminder not to eat lots of raw egg white for months on end.
Streptavidin, a common laboratory protein, is a structural relative of avidin, and the biotin-streptavidin pair is one of the most widely used molecular tagging systems in biotechnology.
Safety · What months of raw egg whites can do
The scene in the Rocky films where Sylvester Stallone drinks raw eggs for breakfast has influenced generations of bodybuilders. But the habit does carry a real risk of biotin deficiency.The case reports tell much the same story: bodybuilders or extreme dieters ate large amounts of raw egg white for a long time (as a protein source, often throwing away the yolks out of fear of cholesterol). After months to years they developed hair loss, skin rash, facial nerve problems, and neuropsychiatric symptoms, and the diagnosis was severe biotin deficiency (a large rise in urinary 3-hydroxyisovaleric acid and a large fall in plasma biotin). They recovered by stopping raw egg white and switching to cooked eggs with the yolk.
The conditions for harm are quite specific: many raw egg whites a day, for months on end. In theory, eating the yolk as well offsets part of it (the yolk contains biotin); the small amount of raw egg white in an occasional eggnog or mousse causes no problem.
It is also true that raw egg protein is less digestible than cooked: Evenepoel 1998 measured it with stable isotopes and found cooked egg protein about 91% digestible versus about 51% for raw, because heat-unfolded protein is easier to digest. "Raw eggs are more nutritious" is a chemistry misunderstanding in fitness circles.
Salmonella is the other real risk of raw eggs. Pasteurized eggs are safer, but they are hard to find in many places.
A few safety recommendations: do not make raw egg white your main protein source; for training, whey, lean meat, or cooked eggs are all safer bets. An egg's nutrients are spread across yolk and white (biotin mostly in the yolk, protein in both), so cook it and eat both. Pregnant women, older adults, and people with weakened immunity are best off avoiding raw eggs entirely.
A note on why the biotin-streptavidin pair matters in science: their bond is among the highest-affinity non-covalent bonds known (Kd about 10⁻¹⁵ M), and it is one of the most widely used tools in molecular biology, in enzyme-linked immunosorbent assays (ELISA), flow cytometry, protein purification, drug delivery, single-molecule sequencing, CRISPR work, and more. Attaching biotin to a molecule (biotinylation) and then catching it with streptavidin is a very common technique in modern biomedical experiments.
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Chapter 4
Elevated pregnancy demand
Pregnancy is a time when biotin status deserves a closer look, but first it is worth being clear about how far the evidence goes.
What has been seen: a review by Mock (2009) found that about half of pregnant women have raised urinary 3-hydroxyisovaleric acid (the urine marker that rises first when biotin runs short), even when their diet looks normal. But pregnancy changes the kidneys in ways that also affect this marker, so it can only say so much; the more cautious summary from the US NIH Office of Dietary Supplements (ODS) is that at least a third of pregnant women develop marginal deficiency. Possible reasons include:
The fetus and placenta actively take up more biotinThe way the kidneys reabsorb it may change in pregnancyCells multiply faster (biotin also takes part in biotinylating histones, which may affect how genes are regulated)
Animal experiments: in mice, a similar degree of marginal deficiency is enough to cause structural defects such as cleft palate, which suggests development is sensitive to it; whether the same holds in people has not been shown.
The adequate intake () in pregnancy is still 30 µg/day; it rises to 35 µg/day only during breastfeeding. Most prenatal multivitamins already contain biotin. The clinical meaning of these biochemical changes is still unclear, so there is currently no recommendation to take extra high-dose biotin in pregnancy.
What has been seen: a review by Mock (2009) found that about half of pregnant women have raised urinary 3-hydroxyisovaleric acid (the urine marker that rises first when biotin runs short), even when their diet looks normal. But pregnancy changes the kidneys in ways that also affect this marker, so it can only say so much; the more cautious summary from the US NIH Office of Dietary Supplements (ODS) is that at least a third of pregnant women develop marginal deficiency. Possible reasons include:
The fetus and placenta actively take up more biotinThe way the kidneys reabsorb it may change in pregnancyCells multiply faster (biotin also takes part in biotinylating histones, which may affect how genes are regulated)
Animal experiments: in mice, a similar degree of marginal deficiency is enough to cause structural defects such as cleft palate, which suggests development is sensitive to it; whether the same holds in people has not been shown.
The adequate intake () in pregnancy is still 30 µg/day; it rises to 35 µg/day only during breastfeeding. Most prenatal multivitamins already contain biotin. The clinical meaning of these biochemical changes is still unclear, so there is currently no recommendation to take extra high-dose biotin in pregnancy.
Clinical · What biotinidase deficiency is
Biotinidase deficiency (BTD) is a rare disease on newborn screening panels, and one of the few inherited diseases that a single vitamin can control.Mechanism: mutations in the BTD gene lower the activity of the enzyme biotinidase. This enzyme recycles used biotin by cutting it off spent carboxylases so it can be used again. Without recycling, the body's biotin keeps falling even on a normal diet.
How common: it is a rare autosomal recessive disease, affecting roughly 1 in several tens of thousands of newborns. It is split into two types by the enzyme activity that remains: below 10% is profound deficiency (profound BTD), and 10–30% is partial deficiency (partial BTD).
Without treatment: children with profound deficiency usually fall ill in infancy (1–12 months), with seizures that are hard to control, low muscle tone, and developmental delay. The typical look is hair loss plus a red, scaly rash around the eyes, nose, and mouth. Hearing and vision loss, metabolic acidosis, and high blood ammonia can follow; the longer it goes untreated, the more permanent the disability, and severe cases can be fatal.
Fortunately, screening and treatment are both well established: the US and many other countries include it in the newborn heel-prick screen. Diagnosed children take 5–10 mg of oral biotin every day for life; started at birth or before symptoms appear, it prevents these symptoms, but hearing loss, vision loss, and developmental delay that have already appeared often do not fully recover. So a positive screening result means seeing a metabolic genetics specialist quickly to confirm the diagnosis and start treatment. One drop of blood buys a lifetime without that disability.
It must be kept clearly apart from marginal deficiency in pregnancy: BTD is an inherited defect, not "eating too little during pregnancy". The adequate intake for ordinary pregnant women is 30 µg/day, which diet plus a prenatal multivitamin usually covers. A biochemical signal such as raised urinary 3-hydroxyisovaleric acid makes sense mechanistically but has limited clinical meaning, and the great majority of pregnant women still have healthy babies.
It is also a reminder that nutrition is not only about what you eat but also about whose body can use it, which is a question of genetics.
Chapter 5
High doses can skew lab tests
High-dose biotin supplements carry an important and often overlooked risk: they interfere with lab tests.
Mechanism: many immunoassays (tests that use antibodies to measure hormones and proteins) rely on biotin and streptavidin, a molecular clasp, to fix the signal in place. When the blood holds a lot of free biotin, it grabs the streptavidin first, and the result is pushed one way or the other depending on how the test is built:
Competitive assays (such as free , FT4, and some hormones): often read falsely highSandwich assays (such as and troponin I / T): often read falsely low
The same marker may be built differently on different platforms, so the lab is the final word on direction.
Real consequences (the FDA's 2017 safety communication): the FDA received a report of a patient on high-dose biotin whose troponin, the test used to diagnose a heart attack, read falsely low; the patient later died. The FDA issued a medical-device safety communication as a result (not a boxed drug warning).
In practice: if you take a supplement with ≥ 5 mg of biotin a day (common in some hair and nail products), stop it at least 48 hours before a lab test and tell your doctor. In an emergency, when there is no time to stop, tell the treating doctor on the spot that you have been taking biotin.
Mechanism: many immunoassays (tests that use antibodies to measure hormones and proteins) rely on biotin and streptavidin, a molecular clasp, to fix the signal in place. When the blood holds a lot of free biotin, it grabs the streptavidin first, and the result is pushed one way or the other depending on how the test is built:
Competitive assays (such as free , FT4, and some hormones): often read falsely highSandwich assays (such as and troponin I / T): often read falsely low
The same marker may be built differently on different platforms, so the lab is the final word on direction.
Real consequences (the FDA's 2017 safety communication): the FDA received a report of a patient on high-dose biotin whose troponin, the test used to diagnose a heart attack, read falsely low; the patient later died. The FDA issued a medical-device safety communication as a result (not a boxed drug warning).
In practice: if you take a supplement with ≥ 5 mg of biotin a day (common in some hair and nail products), stop it at least 48 hours before a lab test and tell your doctor. In an emergency, when there is no time to stop, tell the treating doctor on the spot that you have been taking biotin.
Clinical · Which lab tests can be affected
Below are the specific clinical tests that high-dose biotin (≥ 5 mg/day) can interfere with, roughly grouped by clinical importance. Directions follow the usual assay design; they may differ by platform, and the lab is the final word.Cardiovascular:
Troponin I/T (the marker used to diagnose a heart attack): falsely low, which can miss a heart attack (the main reason for the FDA safety communication)NT-proBNP / BNP (markers of strain on the heart): falsely low, which can miss heart failureD-dimer: may be distorted on some platforms
Endocrine (the most common kind of interference):
: falsely low, which looks like hyperthyroidismFree / free : falsely high, which looks even more like hyperthyroidismParathyroid hormone (): falsely lowCortisol: falsely highSex hormones (, testosterone, progesterone): falsely high on some platforms
Reproduction and pregnancy:
hCG (the pregnancy-test hormone): falsely low, which can miss a pregnancyAFP (alpha-fetoprotein): affected
Tumor markers:
(prostate-specific antigen): may be distorted; the direction depends on the assay platformCA 125, CA 15-3, CA 19-9: may be distorted
Infection-related:
HIV and hepatitis B surface antigen: may be distorted on some platforms25-hydroxyvitamin D: falsely high
Practical advice: anyone taking ≥ 5 mg of biotin a day should stop at least 48 hours before a blood test, and 72 hours is safer if possible; tell your doctor you have taken biotin or a combination product containing it (women's multivitamins and hair and nail supplements often do); different labs use different assay platforms, and the direction of interference can differ, so when results do not match the symptoms, ask the doctor to check with the lab.
This is why biotin is sometimes called one of the cheapest sources of diagnostic confusion: a very cheap pill can lead to a chain of wrong tests, misdiagnoses, and treatments.
References · 8
- National Institutes of Health, Office of Dietary Supplements. (2022). Biotin — Fact Sheet for Health Professionals. Fact sheet (updated January 10, 2022; Wayback snapshot 16 September 2026): adult AI 30 mcg/day, pregnancy 30, lactation 35; at least a third of pregnant women develop marginal biotin deficiency in spite of normal intakes; serum biotin does not fall enough to detect marginal deficiency; Table 2: beef liver, 3 ounces, 30.8 mcg; whole cooked egg 10.0 mcg (fact sheet). ods.od.nih.gov/factsheets/Biotin-HealthProfessional
- Mock, D. M. (2017). Biotin: from nutrition to therapeutics. The Journal of Nutrition, 147(8), 1487-1492. 10.3945/jn.116.238956
- Hochman, L. G., Scher, R. K., & Meyerson, M. S. (1993). Brittle nails: response to daily biotin supplementation. Cutis, 51(4), 303-305. A RETROSPECTIVE chart review: 35 of 44 patients evaluated, 63% reported subjective improvement, no control group. ⚠️ The often-quoted 25% nail-thickness increase is NOT this paper's result — it is its opening sentence citing a Swiss study. pubmed.ncbi.nlm.nih.gov/8477615
- Said, H. M. (2009). Cell and molecular aspects of human intestinal biotin absorption. The Journal of Nutrition, 139(1), 158-162. 10.3945/jn.108.092023
- Mock, D. M. (2009). Marginal biotin deficiency is common in normal human pregnancy and is highly teratogenic in mice. The Journal of Nutrition, 139(1), 154-157. 10.3945/jn.108.095273
- U.S. Food and Drug Administration. (2019, November). The FDA warns that biotin may interfere with lab tests: FDA safety communication. The 2019 update of the 2017 communication: biotin in dietary supplements can significantly interfere with certain lab tests and cause falsely high or falsely low results that may go undetected; FDA is particularly concerned about falsely low troponin results, which may lead to a missed heart-attack diagnosis, and keeps receiving such reports; the daily recommended allowance of 0.03 mg does not typically interfere, but hair, skin and nail supplements may contain high levels (FDA page, Wayback snapshot 19 June 2022). www.fda.gov/medical-devices/safety-communications/update-fda-warns-biotin-may-interfere-lab-tests-fda-safety-communication
- Trambas, C., Lu, Z., Yen, T., & Sikaris, K. (2018). Depletion of biotin using streptavidin-coated microparticles: a validated solution to the problem of biotin interference in streptavidin-biotin immunoassays. Annals of Clinical Biochemistry, 55(2), 216-226. 10.1177/0004563217707783
- Barbesino, G. (2016). Misdiagnosis of Graves' disease with apparent severe hyperthyroidism in a patient taking biotin megadoses. Thyroid, 26(6), 860-863. 10.1089/thy.2015.0664