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Glycine is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐CH2‐COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is the most abundant amino acid in collagen triple-helices
CAS NO: 56-40-6
MF:C2H5NO2
MW: 75.07
EINECS: 200-272-2
Properties
Melting point: 240 °C (dec.)(lit.)
Boiling point: 233°C
Density: 1.595
vapor pressure: 0.0000171 Pa (25 °C)
FEMA 3287 | GLYCINE
refractive index 1.4264 (estimate)
Flash point: 176.67°C
storage temp. 2-8°C
solubility H2O: 100 mg/mL
pka 2.35(at 25℃)
form powder
color <5 (200 mg/mL)(APHA)
Odor Odorless
PH 4(0.2 molar aqueous solution)
PH Range 4
Water Solubility 25 g/100 mL (25 ºC)
Λmax λ: 260 nm Amax: 0.05 λ: 280 nm Amax: 0.05
Merck 14,4491
JECFA Number 1421
BRN 635782
Stability: Stable. Combustible. Incompatible with strong oxidizing agents.
InChIKey DHMQDGOQFOQNFH-UHFFFAOYSA-N
Safety Information
Risk Statements 33
Safety Statements 22-24/25
WGK Germany 2
RTECS MB7600000
TSCA Yes
HS Code 29224910
Toxicity LD50 orally in Rabbit: 7930 mg/kg
Synonms: glycine; 2-Aminoacetic acid; 56-40-6; aminoacetic acid; Glycocoll; Aminoethanoic acid; Glycolixir; Padil; Glycosthene; Aciport; Glicoamin; L-Glycine; H-Gly-OH; Hampshire glycine; Amitone; Leimzucker; Acetic acid, amino-; Aminoazijnzuur; Glycine, non-medical; Sucre de gelatine; Gyn-hydralin; GLY (IUPAC abbrev); Glycinum; Corilin; Glycinum [INN-Latin]; Glicina [INN-Spanish]; Glycine [INN]; glycyl radical; Glyzin; FEMA No. 3287; gly; Acide aminoacetique [INN-French]; Acido aminoacetico [INN-Spanish]; Acidum aminoaceticum [INN-Latin]; CCRIS 5915; HSDB 495; AI3-04085; amino-Acetic acid; UNII-TE7660XO1C; MFCD00008131; NSC 25936; [14C]glycine; CHEMBL773; Glycine iron sulphate (1:1); TE7660XO1C; CHEBI:15428; 2-aminoaceticacid; AZD-4282; NSC25936; Athenon; NSC-25936; polyglycine; NCGC00024503-01; Glicina; DSSTox_CID_667; Glycine, free base; Polyglycine II; Acido aminoacetico; Acide aminoacetique; DSSTox_RID_75720; DSSTox_GSID_20667; Acidum aminoaceticum; Glycine, 99%, ACS reagent; Glycine, 99+%, for analysis; Glykokoll; Aminoessigsaeure; Hgly; CAS-56-40-6; Glycine, labeled with carbon-14; Glycine [USP:INN]; GLYCINE 1.5% IN PLASTIC CONTAINER; EINECS 200-272-2; H2N-CH2-COOH; AMINOACETIC ACID 1.5% IN PLASTIC CONTAINER; Glycine, homopolymer (VAN); Aminoethanoate; amino-Acetate; 2-aminoacetate; Glycine; glycine USP; Glycine Technical; glycine-13c; [3H]glycine; Glycine, EP/USP; H-Gly; L-Gly; Gly-CO; Gly-OH; L-Glycine,(S); [14C]-glycine; Corilin (Salt/Mix); 25718-94-9; Glycine 1 M solution; Tocris-0219; Glycine (H-Gly-OH); NH2CH2COOH; Glycine, >=99%; Glycine (JP17/USP); Glycine, 99%, FCC; Biomol-NT_000195; bmse000089; bmse000977; WLN: Z1VQ; EC 200-272-2; H-[15N]Gly-OH; Gly-253; GTPL727; AB-131/40217813; Glycine, Electrophoresis Grade; BPBio1_001222; GTPL4084; GTPL4635; N[C]C(O)=O; DTXSID9020667; BDBM18133; Buffer Concentrate, pH 11.01; Glycine, >=99.0% (NT); Glycine, 98.5-101.5%; Pharmakon1600-01300021; 2-Aminoacetic acid;Aminoacetic acid; BCP25965; CS-B1641; HY-Y0966; ZINC4658552; Glycine, ACS reagent, >=98.5%; Tox21_113575; 2-amino-1-$l^{1}-oxidanylethanone; ANW-32505; Glycine, 99%, natural, FCC, FG; NSC760120; s4821; STL194276; Glycine, purum, >=98.5% (NT); Glycine, tested according to Ph.Eur.; AKOS000119626; Glycine, for electrophoresis, >=99%; Tox21_113575_1; AM81781; CCG-266010; DB00145; MCULE-2415764032; NSC-760120; Glycine, BioUltra, >=99.0% (NT); Glycine, BioXtra, >=99% (titration); Glycine, SAJ special grade, >=99.0%; NCGC00024503-02; NCGC00024503-03; 18875-39-3; AK-77854; BP-31024; BR-77854; Glycine, Vetec(TM) reagent grade, 98%; Glycine, 0.2M buffer solution, pH 2.5; Glycine, 0.2M buffer solution, pH 3.0; Glycine, 0.2M buffer solution, pH 3.5; DB-029870; FT-0600491; FT-0669038; G0099; G0317; Glycine, ReagentPlus(R), >=99% (HPLC); A20662; C00037; D00011; M-6155; M03001; L001246; Q620730; SR-01000597729; Glycine, certified reference material, TraceCERT(R); Q-201300; SR-01000597729-1; Q27115084; B72BA06C-60E9-4A83-A24A-A2D7F465BB65; F2191-0197; Glycine, European Pharmacopoeia (EP) Reference Standard; Z955123660; Glycine, BioUltra, for molecular biology, >=99.0% (NT); UNII-0O72R8RF8A component DHMQDGOQFOQNFH-UHFFFAOYSA-N; Glycine, United States Pharmacopeia (USP) Reference Standard; Glycine, Pharmaceutical Secondary Standard; Certified Reference Material; Tris-tricine buffer; Tris-glycine buffer;Tris glycine buffer concentrate; Glycine, analytical standard, for nitrogen determination according to Kjeldahl method; Glycine, from non-animal source, meets EP, JP, USP testing specifications, suitable for cell culture, >=98.5%; Glycine, meets analytical specification of Ph. Eur., BP, USP, 99-101% (based on anhydrous substance); Glycine, PharmaGrade, Ajinomoto, EP, JP, USP, manufactured under appropriate GMP controls for Pharma or Biopharmaceutical production, suitable for cell culture; Glycine, puriss. p.a., Reag. Ph. Eur., buffer substance, 99.7-101% (calc. to the dried substance)
Glycine is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable), with the chemical formula NH2‐CH2‐COOH. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). Glycine is integral to the formation of alpha-helices in secondary protein structure due to its compact form. For the same reason, it is the most abundant amino acid in collagen triple-helices. Glycine is also an inhibitory neurotransmitter – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited muscle contraction. Glycine is a colorless, sweet-tasting crystalline solid. It is the only achiral proteinogenic amino acid. It can fit into hydrophilic or hydrophobicenvironments, due to its minimal side chain of only one hydrogen atom. The acyl radical is glycyl.
Glycine is an amino acid, a building block for protein. It is not considered an “essentialamino acid” because the body can make it from other chemicals. A typical diet contains about 2 grams of glycine daily. The primary sources are protein-rich foods including meat, fish, dairy, and legumes. Glycine is used for treating schizophrenia, stroke, benign prostatic hyperplasia (BPH), and some rare inherited metabolic disorders. It is also used to protect kidneys from the harmful side effects of certain drugs used after organ transplantation as well as the liverfrom harmful effects of alcohol. Other uses include cancer prevention and memoryenhancement. Some people apply glycine directly to the skin to treat leg ulcers and heal other wounds. The body uses glycine to make proteins. Glycine is also involved in the transmission of chemical signals in the brain, so there is interest in trying it for schizophrenia and improving memory. Some researchers think glycine may have a role in cancer prevention because it seems to interfere with the blood supply needed by certain tumors. Glycine has numerous proposed uses. Few of those suggested uses have enough evidence to fully back glycine's effectiveness. Glycine, the simplest amino acid, obtainable by hydrolysis of proteins. Sweet-tasting, it was among the earliest amino acids to be isolated from gelatin (1820). Especially rich sources include gelatin and silk fibroin. Glycine is one of several so-called nonessential amino acids for mammals; i.e., they can synthesize it from the amino acids serine and threonine and from other sources and do not require dietary sources.
Glycine has shown the most promise as a part of a treatment plan for schizophrenia. In several studies, glycine boosted the effectiveness of other schizophrenia drugs when taken at doses of .6 grams per kilogram of weight per day. However, glycine may have the opposite effect when paired with the antipsychotic drug clozapine (Clozaril, Versacloz).
A small study suggests that glycine may help people with type 2 diabetes control their blood sugar. But more research is needed to back up that result.
In a much larger study, small doses of glycine (1 to 2 grams dissolved under the tongue each day) showed some potential for limiting brain damage caused by ischemic stroke if treatment begins within several hours of a stroke. There is some concern, though, that high doses of glycine could make the damage caused by a stroke worse. Glycine is a non-essential amino acid that is produced naturally by the body. It is one of 20 amino acids in the human body that synthesize proteins, and it plays a key role in the creation of several other important compounds and proteins. It has been shown to be safe as a dietary supplement, although a healthy and varied diet will typically provide the necessary amounts of glycine the body needs.
It is thought that glycine (among other non-essential amino acids) helps bone health through the production of insulin and insulin-like growth factor 1, along with the synthesis of collagen, which is an important protein for bone, tissue, and muscle health throughout the body.
Boosting creatine in the muscles can help them to perform better in short, intense bursts of activity such as weightlifting or sprinting. Several studies have shown that boosting creatine in the body can lead to increased muscle strength, mass, and power, and it may also help with recovery after exercise and rehabilitation after injury.
One study found that a daily dose of 5 g to 20 g of creatine meant that patients requiring one injured leg to be kept in a cast for 2 weeks experienced less muscle atrophy due to inactivity, and they gained more strength from their rehabilitation exercises than those not taking creatine.
As a result, glycine is a popular supplement for bodybuilders and those wishing to gain muscle mass and strength. However, the body can synthesize creatine itself and can be taken in through the diet, so glycine supplements to boost creatine levels may not always be necessary.
Glycine supplements have been shown to reduce the levels of bone loss in osteopenic postmenopausal women, reduce joint deterioration in athletes experiencing joint pain, and increase skin elasticity in older women.
3 g of glycine a day before sleep has been found to improve sleep quality and reduce feelings of fatigue during the day in people with insomnia or those who do not have much time to sleep.
Glycine injections in animal studies have been shown to limit the activity of neurons that are responsible for arousal and energy homeostasis, and glycine injections have also been found to encourage non-REM sleep in mice, although the link between glycine and neuronal activity blocking of this kind is disputed.
Sleep may also be improved with glycine because it decreases the body’s core temperature, and cooler body temperatures are linked with better quality sleep.
It is believed that glycine supplementation activates N-methyl-D-aspartate (NMDA) receptors in the suprachiasmatic nucleus (SCN) and leads to better thermoregulation and circadian rhythm, although the mechanisms through which glycine activates NMDA receptors in the SCN to induce better sleep are not yet understood.
Glycine is also an inhibitory neurotransmitter in the central nervous system and plays a role in the processing of motor and sensory information. It is found in the spinal cord, the brainstem, and the retina, and can both inhibit and promote excitability in various neurotransmitters.
This can be helpful and dangerous depending on the strength of inhibition or excitation and the dose of glycine.
If a dose of glycine is too high, it can cause fatal hyperexcitability in the brain, but highly inhibited glycine can cause muscular convulsions and asphyxia, causing death. This is because glycine receptors can be blocked by strychnine, which in high amounts causes these fatal complications.
However, the inhibitory functions of glycine help manage psychological conditions such as schizophrenia, and glycine has become a potential therapeutic route for the management of schizophrenia symptoms.
Glycine can increase the neurotransmission of NMDA, and low levels of NMDA receptors have been reported as a possible contributing factor to the development of schizophrenia. Glycine is safe for short- and long-term use, and as such it is a possible effective treatment for the symptoms of schizophrenia.
Literature reviews have found that creatine supplements may improve short-term memory function and the reasoning capabilities in healthy people, although its benefits on those living with dementia or other degenerative cognitive diseases have not been fully ascertained.
Related to glycine’s role in the creation of creatine, it has been widely documented that creatine has neuroprotective properties. Animal studies investigating the benefits of creatine supplementation on traumatic brain injuries (TBI), cerebral ischemia, and spinal cord injuries (SCI) have found that creatine can improve the level of damage to the cortical region from 36 to 50 percent, and in rats with spinal cord injuries, creatine supplementation improved locomotor function. As it has been proven safe to consume as a supplement, creatine supplementation could, therefore, have potential as a therapeutic agent in humans to treat TBI and SCI. Although glycine is made naturally by the body, it can also be found in a range of common foods, including meat, fish, dairy products, and legumes. These protein-rich foods should provide the body with enough glycine to function healthily without the need for glycine supplementation. Glycine supplements are made in powders or capsules, and powders are often added to food and drinks because of their naturally sweet taste.
Glycine is an amino acid commonly found in proteins. It is synthesized in the body from serine, another proteinogenic amino acid naturally synthesized within cells. As one of the 20 most common amino acids found in proteins, it serves multiple metabolic functions, but some of it is also released into synapses as a neurotransmitter.
Levels of glycine are primarily regulated by enzymatic degradation. Various enzymes are responsible for the breakdown of glycine. Some of these processes reverse the metabolism of glycine and convert the amino acid back to serine. Other enzymatic processes transform glycine into other molecules, including gloxylic acid.
Like glutamate and GABA, glycine is present in the nervous system and is an important building block for many chemical processes. As a neurotransmitter, it binds to several families of ionotropic and metabotropic receptors, but its primary inhibitory action seems to be the result of regulating chloride channels in a manner similar to the action of GABA. These effects are primarily seen in the spinal cord. In the brain, the effects of glycine are less predictable. For example, it seems to be involved in regulating glutamatergic neurotransmission at the NMDA glutamate ionotropic receptors that are involved in opening calcium channels and causing rapid depolarization of the post-synaptic cell. Thus, glycine may be an alosteric modulator for glutamate.
Increase in glycine function may result in effects similar to the increase of GABAergic neurotransmission (fatigue, drowsiness, etc.). However, since glycine seems to have varying effects in different parts of the brain, supplementation with glycine may also result in excitatory effects. For example, in overdose, glycine causes death by hyperexcitability of the brain. Supplementation with glycine seems to offer limited benefits, although some preliminary evidence exists that it may be helpful in treating the symptoms of psychosis
Inhibition of glycine action is also associated with serious risks. Strichnine is a potent glycine antagonist, and causes muscular convulsions and death by asphyxia. In smaller doses, it was once used as a stimulant. Interestingly, bicuculine is a weaker antagonist that seems to exert its effect by antagonizing glycine and GABA. Thus, the effects of the inhibition of glycine may be similar to those seen when GABA transmissions are antagonized.
History:
Glycine was discovered in 1820 by the French chemist Henri Braconnot when he hydrolyzed gelatin by boiling it with sulfuric acid.[7] He originally called it "sugar of gelatin",[8][9] but the French chemist Jean-Baptiste Boussingault showed that it contained nitrogen.[10] The American scientist Eben Norton Horsford, then a student of the German chemist Justus von Liebig, proposed the name "glycocoll"; however, the Swedish chemist Berzelius suggested the simpler name "glycine". The name comes from the Greek word γλυκύς "sweet tasting" (which is also related to the prefixes glyco- and gluco-, as in glycoprotein and glucose). In 1858, the French chemist Auguste Cahours determined that glycine was an amine of acetic acid.
Produc Although glycine can be isolated from hydrolyzed protein, this is not used for industrial production, as it can be manufactured more conveniently by chemical synthesis. The two main processes are amination of chloroacetic acid with ammonia, giving glycine and ammonium chloride, and the Strecker amino acid synthesis, which is the main synthetic method in the United States and Japan. About 15 thousand tonnes are produced annually in this way.
Glycine is also cogenerated as an impurity in the synthesis of EDTA, arising from reactions of the ammonia coproduction.
Glycine is an inhibitory neurotransmitter in the brainstem and spinal cord.
Glycine and GABA receptors may mediate the effects of inhaled anesthetics.
It is a nonessential amino acid sold as a natural sugar substitute, a sedative, an antacid; to promote muscle growth, ↓ Sx of BPH, as an polyphenol, and antipsychotic.
Glycine 1.5% used as a nonhemolytic irrigation solution during TURP.
Antagonists of glycine binding to NMDA receptor complex are used as anticonvulsants.
Attempts to use glycine and other NMDA agonist in schizophrenia have had little success.
Intrathecal glycine is not different than placebo in CRPS treatment.
Glycine can be metabolized to glyoxylate, a precursor of oxalate. Intravenous infusion of 1 liter of 2.2% glycine, 1.5% glycine + 1% ethanol, or 5% mannitol on 13 occasions in five healthy volunteers and glycine irrigation in nine patients undergoing transurethral prostatic did not increase urinary oxalate concentrations. In 10 male volunteers there was no change in urinary excretion of oxalate, calcium, or citrate after an intravenous infusion of glycine 22 g, although urine volume and amino acid excretion increased.
Although glycine is the simplest amino acid, it has a complex array of functions and effects on the body. While it can inhibit certain neurotransmitters that can improve certain psychological conditions, it can also excite neurotransmitters that cause muscular convulsions and potentially fatal brain hyperexcitability.
It is safe to consume as a dietary supplement in appropriate doses, both for short- and long-term use, however, the body will usually receive the right amount of glycine from a varied, healthy diet. It has a range of benefits that include the bones, tissues, muscles, and central nervous system, and as such is one of the most important non-essential amino acids in the body.
