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DL-isoleucine is the racemic form of isoleucine, composed of equal amounts of L-type and D-type mirror-image molecules. As a branched-chain amino acid with two chiral centers, its unique structure combines the chirality of the β-carbon atom and the methyl-butanyl backbone of the hydrophobic side chain. This complex spatial arrangement makes it an ideal model for physicochemical property studies.
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| Chemical Formula | C6H13NO2 |
| Molecular Weight | 131.17 |
| Exact Mass | 131.09 |
| m/z | 131.09 (100.0%), 132.10 (6.5%) |
| Elemental Analysis | C, 54.94; H, 9.99; N, 10.68; O, 24.39 |
| Melting point | 290 °C (dec.) (lit.) |
| Boiling point | 225.8±23.0 °C(Predicted) |
| Storage conditions | Keep in dark place,Inert atmosphere,Room temperature |
| Form | Powder |
| Color | White |
| Solubility | Stable. Incompatible with strong oxidizing agents. |
| Water solubility | 22.3 g/L (25 ºC) |
At the biochemical level, although only the L-type can be directly used by organisms for protein synthesis and metabolic regulation, the coexistence of the D-type significantly alters the crystallization habit, dissolution kinetics, and phase transition behavior, providing a classic example for the development of chiral separation techniques. This racemic form serves as a key indicator in industrial fermentation process optimization, allowing for precise assessment of the stereoselectivity of the strain by monitoring its dynamic equilibrium. At the same time, it is introduced as a non-natural structural unit into synthetic peptide chains to regulate conformational stability, and in the field of pharmaceuticals, it serves as a chiral separation reagent and standard substance, profoundly promoting the development of chiral drug analysis and asymmetric synthesis methodologies.
Although DL-Isoleucine does not exist in pure DL form in nature (mainly in the form of L-DL Isoleucine), in certain application fields, DL Isoleucine or its mixtures may have specific uses.
The following are possible application areas of DL Isoleucine:
Biochemical research:
DL Isoleucine may be used as an experimental reagent in biochemical and molecular biology research to study the metabolic pathways of amino acids, enzymatic reactions, and protein synthesis processes. Although L-DL Isoleucine is more commonly used in these studies, DL Isoleucine may also be effective under specific experimental conditions.
Drug synthesis:
DL Isoleucine or its derivatives may be used as starting materials or intermediates in certain drug synthesis processes. However, this situation is relatively rare because drug synthesis usually has strict requirements for the purity and stereoconfiguration of the raw materials.
Although the uses of DL Isoleucine are not as extensive and specific as its pure L-form, it still has certain application value in certain fields.
The following are possible uses of DL Isoleucine:
Nutritional supplements and feed additives
DL Isoleucine may be used as a part of mixed amino acids in nutritional supplements to provide comprehensive amino acid support, especially for those who require additional amino acid supplementation, such as athletes, fitness enthusiasts, and the elderly.
DL Isoleucine or its mixture can be used as a nutritional enhancer in animal feed, promoting animal growth and development, increasing feed conversion rate, thereby reducing costs and improving breeding efficiency.
Biochemical research
DL Isoleucine can be used as an experimental reagent in biochemical and molecular biology research to study the metabolic pathways of amino acids, enzymatic reaction mechanisms, and protein synthesis processes. Although pure L-DL Isoleucine is more commonly used in these studies, DL Isoleucine may also play an important role under certain specific experimental conditions.
Drug synthesis intermediates
DL Isoleucine or its derivatives may be used as starting materials or intermediates in certain drug synthesis processes. Although this situation is relatively rare, DL Isoleucine may have unique reactivity and selectivity in certain specific drug synthesis pathways.
Cosmetics and skincare products
Although the direct application of DL Isoleucine in cosmetics and skincare products is not widespread, some advanced skincare products may utilize the moisturizing, antioxidant, and reparative functions of amino acids to incorporate DL Isoleucine or its analogues as part of their formula. These amino acid components help improve skin texture, enhance skin barrier function, and promote skin health.
DL Isoleucine and leucine are both essential amino acids for the human body, and there are some differences in their chemical structure, function, and use.
The main differences between DL Isoleucine and leucine are as follows:
1.Chemical Structure
DL-Isoleucine
Chemical name 2-amino-3-methylvaleric acid, is an organic compound with the chemical formula C6H13NO2. It belongs to branched chain amino acids with optical activity, and the side chain is sec butyl (i.e. 2-methylpropyl).
Leucine
Its chemical name is 2-amino-4-methylpentanoic acid, and it is also an organic compound with the chemical formula C6H13NO2. It is also a branched amino acid, but the side chain is isobutyl (i.e. 2-methyl-2-propyl).
2.Function
DL-Isoleucne
Promote protein synthesis, increase growth hormone and insulin levels.
Enhance the body's immune function and maintain balance.
Treat mental disorders, promote increased appetite, and combat anemia.
Promote insulin secretion and regulate blood sugar levels.
Plays an important role in muscle protein metabolism, promoting muscle recovery after training.
Protect body tissues from external environmental damage and promote the healing of tissues such as bones and skin.
Has antioxidant properties, clears free radicals, and reduces the damage of oxidative stress reactions to the human body.
Leucine
Leucine also promotes protein synthesis, but its main characteristic is that it can be broken down and converted into glucose more quickly, effectively preventing muscle loss.
Leucine also plays a certain role in regulating blood sugar and promoting wound healing.
3.Application and Source
DL-Isoleucne
Mainly used in the pharmaceutical and food industries, it has hepatoprotective and hepatoprotective effects.
As a feed additive, it enhances the growth and development rate of animals and increases the production of meat and dairy products.
Used in biotechnology for synthesizing important proteins and peptide compounds.
It can also be used as an organic crystal material with good optical properties and potential applications in electronic devices.
Foods rich in DL Isoleucine include eggs, chicken, lamb, pork, soybeans, milk, cheese, grains, cashews, and more.
Leucine
It is also widely used in fields such as medicine, food, and feed.
Foods rich in leucine include dairy products, meat (such as beef, pork, chicken), fish, beans (such as soybeans, peas), etc.
4. Other
Both are branched chain amino acids (BCAAs), but DL-Isoleucine has a moderate ability to promote muscle protein synthesis, stronger than valine but much weaker than leucine.
Both are mainly concentrated in muscle tissue in the human body and participate in the synthesis of hemoglobin, which helps to transport oxygen from the lungs to human tissues.
In summary, DL Isoleucine and leucine have their own characteristics in chemical structure, function, and application, but they are both essential amino acids for the human body. With a balanced diet, the human body can obtain sufficient amounts of these two amino acids from a variety of foods.
The main differences between the D, L, and DL forms of DL isoleucine are as follows:
Structural differences
D-type isoleucine:
Isoleucine with a D-configuration, where the D-configuration indicates that the chirality (enantiomer) of the compound is right-handed.
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L-type isoleucine:
Isoleucine with an L-configuration, where the L-configuration indicates that the chirality of the compound is left-handed.
DL type isoleucine:
Isoleucine that contains both D-configuration and L-configuration, is a racemic form, which is a mixture of two conformations.
Biological activity and utilization
D-type isoleucine:
Relatively rare in nature, it may have specific effects in certain biological processes, but enzymes in organisms are usually selective for the chirality of D-type amino acids, so D-type isoleucine is rarely directly utilized by organisms.
L-type isoleucine:
It is a common form of amino acid in living organisms and is a fundamental component of proteins. It is essential for the normal functioning of living organisms. L-type isoleucine is linked together by peptide bonds to form polypeptide chains, which then form protein molecules and participate in metabolic processes, regulate physiological functions, and construct cellular structures.
DL type isoleucine:
Due to containing both D and L conformations, it usually does not have biological activity. DL type amino acids are rarely found in living organisms and are mainly used in laboratory research, such as preparing tissue culture media.
Adverse reactions
DL Isoleucine is a chemically synthesized branched chain amino acid with high solubility in hot ethanol and hot acetic acid, but insoluble in ether. In terms of physiological function, isoleucine is one of the essential amino acids in the human body, involved in protein synthesis, energy metabolism, and immune regulation. L-Isoleucine plays an important role in maintaining muscle mass, exercise endurance, and wound repair by promoting insulin secretion, regulating blood glucose levels, and serving as a key raw material for muscle protein synthesis.
However, DL isoleucine, as a racemic mixture (containing 50% L-isoleucine and 50% D-isoleucine), its D-isomer cannot be effectively utilized in the human body and may affect the normal function of L-isoleucine through competitive inhibition or metabolic interference, leading to adverse reactions.
Classification and mechanism of adverse reactions
Digestive system response
Excessive intake of DL isoleucine may directly irritate the gastric mucosa, causing symptoms such as nausea, vomiting, abdominal pain, and diarrhea. The mechanism may be related to the following factors:
Osmotic pressure effect: High concentration amino acid solutions can alter intestinal osmotic pressure, causing water to transfer into the intestinal lumen and leading to osmotic diarrhea.
Metabolite stimulation: D-isoleucine may be broken down by bacteria in the intestine into short chain fatty acids or other metabolites, directly stimulating the intestinal mucosa and inducing inflammatory reactions.
Competitive inhibition: D-isoleucine may competitively inhibit the transport carrier of L-isoleucine (such as B ⁰ AT1), reduce the absorption of L-isoleucine, lead to the accumulation of unabsorbed amino acids in the intestine, and further increase the burden on the gastrointestinal tract.
Digestive system response
Long term excessive intake of DL isoleucine may increase the metabolic burden on the liver, leading to elevated levels of transaminases such as ALT and AST, and even causing liver cell damage. The mechanism may be related to the following processes:
Imbalance in amino acid metabolism: D-isoleucine cannot enter the tricarboxylic acid cycle and may generate large amounts of ammonia or toxic metabolites through other pathways (such as transamination), increasing the detoxification burden on the liver.
Oxidative stress: D-isoleucine metabolism may produce excessive reactive oxygen species (ROS), leading to lipid peroxidation and DNA damage in liver cells.
Drug interactions: DL isoleucine may compete with certain drugs (such as antiepileptic drugs and antibiotics) for metabolic enzymes (such as CYP450), affecting drug metabolism and indirectly leading to liver damage.
Neurological response
High doses of amino acids may affect endothelial function, leading to cerebral vasodilation and causing headaches. D-isoleucine may interfere with neurotransmitter synthesis involving L-isoleucine (such as gamma aminobutyric acid, glutamate), leading to changes in central nervous system excitability. Long term excessive intake may lead to abnormal levels of blood sodium and potassium, affecting the membrane potential of nerve cells and causing dizziness. A very small number of individuals may develop allergic reactions to DL isoleucine, manifested as rash, itching, difficulty breathing, and even anaphylactic shock. The mechanism is:
Metabolism and endocrine response
L-isoleucine can promote insulin secretion in pancreatic beta cells, but D-isoleucine may interfere with this process, leading to abnormal insulin secretion and causing hypoglycemia or hyperglycemia. High doses of amino acids may inhibit hepatic gluconeogenesis, reduce blood glucose sources, and increase the risk of hypoglycemia, especially after fasting or prolonged exercise. Long term excessive intake may lead to decreased insulin sensitivity in muscle and adipose tissue, inducing insulin resistance.
DL isoleucine metabolism may produce acidic or alkaline metabolites, affecting the acid-base balance in the body: D-isoleucine may generate acidic substances such as sulfates and phosphates through incomplete metabolism, leading to metabolic acidosis. High doses of amino acids may competitively inhibit renal tubular reabsorption of bicarbonate, exacerbating the risk of acidosis.
DL-Isoleucine, also known as DL-isoleucine (CAS: 443-79-8), is an important racemic amino acid composed of D-isoleucine and L-isoleucine, and its discovery history is closely linked to the exploration of isoleucine and the development of amino acid chemistry in the early 20th century. Its discovery process is a gradual deepening from the identification of natural isoleucine to the synthesis of its racemic form, reflecting the continuous progress of early organic chemistry and biochemistry research.
In 1903, German chemist Felix Ehrlich first discovered isoleucine while studying the composition of beet-sugar molasses, laying the foundation for the subsequent discovery of DL-Isoleucine. In 1905, French chemists Bouveault and Locquin reported the first synthesis of isoleucine, which provided a feasible technical path for the preparation of racemic isoleucine. In 1907, Ehrlich further verified the natural composition of isoleucine through studies on fibrin, egg albumin and other proteins, and published his own synthesis method of isoleucine in 1908, further improving the synthesis technology of isoleucine derivatives.
As a racemic mixture, DL-Isoleucine was gradually recognized and prepared in the process of isoleucine research. Early chemists found that the racemic form synthesized by chemical methods had the advantages of simple process and low cost, which was different from the L-isoleucine extracted from natural substances. With the development of amino acid separation and purification technology, DL-Isoleucine was successfully separated and purified, and its chemical structure was confirmed by spectral analysis.
In the following decades, the synthesis process of DL-Isoleucine was continuously optimized, and its application value in feed, food and pharmaceutical fields was gradually explored. Its discovery not only enriched the types of amino acid derivatives, but also provided an important raw material for industrial production and scientific research, laying a foundation for the development of related fields such as biochemistry, nutritional science and organic synthesis.
FAQ
How can I lower my isoleucine intake?
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Modify Your Meals: Focus on eating foods low in isoleucine during these designated periods. Increase your intake of fruits, vegetables, and grains, which are generally lower in isoleucine compared to animal proteins and certain nuts and seeds.
What happens if you have too much isoleucine?
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Remember, while isoleucine is important for your health, having too much can throw off your body's balance. Symptoms of high levels of Isoleucine are typically not distinct, as they can overlap with symptoms of other conditions. However, they could potentially include fatigue, irritability, or muscle weakness.
Does peanut butter have isoleucine?
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Peanut butter is rich in leucine and phenylalanine, has moderate amounts of tyrosine, valine, lysine, isoleucine, and threonine, and contains lower amounts of histidine and tryptophan.
Is yogurt high in isoleucine?
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Milk, cheese, and especially Greek yogurt, are valuable sources of isoleucine. They also provide calcium and probiotics, essential for bone health and digestion.
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