Herpes, lysine and amino acid antagonism

The absorption of free amino acids takes place through active transport. This means that it requires energy and a carrier. The energy is provided by the sodium pump.

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What is amino acid antagonism?

The individual amino acids compete for the carrier substance with glucose and free amino acids. The antagonism of the amino acids is because lysine, for example, utilises the same carrier substance as arginine. An overdose of lysine can therefore lead to an arginine deficiency.

There is also antagonism between threonine and tryptophan and similar competition between threonine and valine. There are many amino acid antagonisms, the consequences of which are difficult to understand. An imbalance of amino acids can be a problem due to antagonism. Some amino acids have significant toxicological effects, such as tyrosine.

Herpes virus and lysine

The anti-herpesviral effect of lysine is based on the physiological effect of amino acid antagonism. Lysine prevents the absorption of arginine. The herpes virus cannot multiply in the absence of arginine and the clinical symptoms disappear within 2-3 hours. Just 2 grams of lysine prevent the virus from replicating. The lysine-arginine antagonism is very high. The cause of the occurrence of herpes viruses is immunosuppression. Lysine does not inhibit virus replication when ingested with natural protein with a high lysine content (e.g. in meat), as it is accompanied by significant amounts of arginine. Only free amino acid lysine has an inhibitory effect. Natural protein does not contain lysine as a free amino acid but in the form of di- and tripeptides.

Where and how is protein absorbed?

The predominant form of peptide absorption is the adsorption of di- and tripeptides. The final hydrolysis of these peptides takes place in the mucosal cells of the small intestine by peptidases. As a result, only free amino acids enter the portal circulation. The absorption of amino acids is therefore more optimal from dipeptides than from free amino acids.

Numerous free amino acids have a medicinal effect, such as tryptophan, which acts as an excellent sleeping pill, analgesic and antidepressant. Phenylalanine is an anxiolytic and antidepressant that increases sexual desire.

In addition, numerous physiological changes have been described for arginine, ornithine, glutamine, glutamic acid, aspartic acid, cystine, cysteine, glycine, methionine and tyrosine, which are classified as drug effects.

The following quote by Earl Mindell from a book on dietary supplements and vitamins is worth quoting: Regarding amino acid supplements, the author warns against using them regularly as a substitute for food, taking them in extremely high doses, or administering them in place of medication without a doctor’s advice. It is recommended to always keep these products away from children.

Absorption of carbohydrates

The body favours disaccharides over monosaccharides when absorbing carbohydrates. Similar to the absorption of dipeptides and amino acids, disaccharides are absorbed quickly and passively. Monosaccharides, on the other hand, are absorbed in a slower, energy-intensive process that requires an active carrier molecule before they enter the portal circulation.

Glucose is a monosaccharide that can inhibit the absorption of amino acids
The glucose-carrying molecule is the same as lysine. Intensive glucose intake interrupts the transport of amino acids. It is therefore unfavourable to consume monosaccharides such as glucose or fructose and high amounts of free amino acids at the same time, as glucose can also be an obstacle to the absorption of amino acids.

Amino acids can also be toxic

The pathophysiology of amino acid toxicity has not yet been sufficiently researched. This makes it all the more important for professionals to act responsibly when using fermented and synthetic amino acids. It is therefore of great importance to carefully monitor the use of amino acids.

The relationships are complex: amino acids that are affected by antagonism pass through the digestive tract in a distal direction without being absorbed. Due to the antagonism of amino acids, free amino acids are more easily attacked by the decarboxylase enzyme. This enzyme is produced by harmful intestinal bacteria (E. coli, Salmonella sp. and Clostridium sp.) that have multiplied in dysbiosis.

Up to 80% of the anabolic proteins are absorbed in the intestine as dipeptides. Non-absorbed anabolic proteins are most frequently present in the intestinal contents in the form of di- and tripeptides. The unabsorbed free amino acid can be converted directly into biogenic amines by the activity of the enzyme decarboxylase. These can therefore be better converted into biogenic amines than other amino acids.

The following biogenic amines can be derived from each amino acid:

  • Arginine is converted to agmatine
  • Ornithine is converted to putrescine and lysine to cadaverine
  • Methionine is converted to spermine and spermidine
  • In the urea cycle, arginine is formed from ornithine
  • Tryptophan becomes serotonin
  • Phenylalanine to phenylethylamine
  • Tyrosine to tyramine

In the pathophysiological and metabolic literature on amino acid toxicity, one often finds the statement: “In recent years, research has focused on explaining diseases associated with amino acid imbalances. Astonishingly, the body’s metabolism can be disturbed by the intake or withdrawal of small amounts of amino acids. However, the body easily oxidises proteins that are supplied in excess in large quantities.”

Endogenous and exogenous biogenic amines

Amines are known as biogenic amines. Many of them have important biological functions and are known as tissue hormones. There are endogenous and exogenous biogenic amines. Endogenous biogenic amines are produced in various organs under controlled conditions and play an important role in the fine regulation of the body. They have several physiological functions. They regulate blood pressure and the secretion of hydrochloric acid in the stomach. They are involved in the transmission of stimuli and control many physiological processes through finely tuned neuronal regulation. They are also neurotransmitters.

Histamine is a biogenic amine derived from histidine. Tyramine is derived from tyrosine, serotonin and tryptamine from tryptophan, cadaverine from lysine (cadaverine), γ-aminobutyric acid from glutamic acid, putrescine from ornithine and arginine.

Read the article in German: Herpes, Lysin und Aminosäureantagonismus

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