PROAMINO-L POWDER
L-lysine
What it does
L-lysine is an essential amino acid that your body needs to build proteins and support various bodily functions.
Commonly used for: cold sores (herpes simplex), supporting immune function, promoting muscle recovery
Read more in plain English ↓Plain-language summary for general understanding - not medical advice. Always follow your pharmacist/doctor.
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Sourcing - Kenya onlyRegistration & product details
Source: Food and Drugs Authority · fetched 2026-04-18 08:37:32 · updated 2026-10-20 04:00:06
About this medicine
L-lysine is an essential amino acid that your body needs to build proteins and support various bodily functions.
What it treats
- cold sores (herpes simplex)
- supporting immune function
- promoting muscle recovery
How it works
L-lysine helps your body produce proteins and is important for growth and maintenance.
Who it's for
L-lysine is suitable for adults and children who need extra support for their immune system or muscle recovery.
AI-assisted summary grounded in BNF data - general information only, not medical advice. Always confirm with your pharmacist or doctor.
Clinical monograph: llysine
BNF-referencedLysine is an essential amino acid that plays a critical role in protein synthesis and various metabolic functions. It is vital for the production of proteins, collagen, hormones, and enzymes. Additionally, lysine is known to inhibit the replication of herpes simplex virus when present in higher concentrations relative to L-arginine, providing potential therapeutic benefits for managing herpes infections. It also aids in calcium absorption and is necessary for proper growth and development.
Indications
- Herpes simplex virus infections
- Lysine deficiency
- Support in calcium absorption
- Collagen synthesis
Dosage
Children: Refer to the BNF for Children for specific paediatric dosing guidelines.
Adults: Refer to the BNF for specific adult dosing guidelines.
Mechanism of action
Lysine inhibits the replication of herpes simplex virus by altering the amino acid ratio in tissues, particularly decreasing the availability of L-arginine which the virus requires for replication. Additionally, lysine is involved in protein synthesis where it binds with transfer RNA (tRNA) to facilitate the translation process that produces specific proteins.
Pharmacodynamics
Lysine ensures the adequate absorption of calcium, supports collagen formation which is essential for bone, cartilage, and connective tissues, and aids in the production of antibodies, hormones, and enzymes. A deficiency in lysine can lead to various health issues including fatigue, concentration difficulties, irritability, and reproductive problems.
Pharmacokinetics
Lysine is rapidly absorbed from the gastrointestinal tract. It is distributed throughout the body and is primarily excreted via the kidneys. The half-life and detailed metabolic pathways of lysine can vary based on individual physiological conditions and dietary intake.
Adverse effects
- Gastrointestinal disturbances
- Abdominal pain
- Nausea
- Diarrhea
Precautions
- Use with caution in individuals with kidney disease
- Monitor for gastrointestinal effects
Pregnancy
L-lysine is generally considered safe during pregnancy, but clinical advice should be sought.
Breast-feeding
L-lysine is excreted in breast milk, but is typically deemed safe during breastfeeding.
Storage
Store in a cool, dry place away from direct sunlight.
Formulations
- Tablets
- Capsules
- Powder
AI-synthesized from BNF references - general information only, not a substitute for professional medical advice or the current BNF. Verify doses with a pharmacist.
Molecular reference: l-lysine
PubChem CID 5962Molecular formula: C6H14N2O2
Mechanism of action
Proteins of the herpes simplex virus are rich in L-arginine, and tissue culture studies indicate an enhancing effect on viral replication when the amino acid ratio of L-arginine to lysine is high in the tissue culture media. When the ratio of L-lysine to L-arginine is high, viral replication and the cytopathogenicity of herpes simplex virus have been found to be inhibited. L-lysine may facilitate the absorption of calcium from the small intestine. Amino acids are selected for protein synthesis by binding with transfer RNA (tRNA) in the cell cytoplasm. The information on the amino acid sequence of each individual protein is contained in the sequence of nucleotides in the messenger RNA (mRNA) molecules, which are synthesized in the nucleus from regions of DNA by the process of transcription. The mRNA molecules then interact with various tRNA molecules attached to specific amino acids in the cytoplasm to synthesize the specific protein by linking together individual amino acids; this process, known as translation, is regulated by amino acids (e.g., leucine), and hormones. Which specific proteins are expressed in any particular cell and the relative rates at which the different cellular proteins are synthesized, are determined by the relative abundances of the different mRNAs and the availability of specific tRNA-amino acid combinations, and hence by the rate of transcription and the stability of the messages. From a nutritional and metabolic point of view, it is important to recognize that protein synthesis is a continuing process that takes place in most cells of the body. In a steady state, when neither net growth nor protein loss is occurring, protein synthesis is balanced by an equal amount of protein degradation. The major consequence of inadequate protein intakes, or diets low or lacking in specific indispensable amino acids relative to other amino acids (often termed limiting amino acids), is a shift in this balance so that rates of synthesis of some body proteins decrease while protein degradation continues, thus providing an endogenous source of those amino acids most in need. /Amino acids/ The mechanism of intracellular protein degradation, by which protein is hydrolyzed to free amino acids, is more complex and is not as well characterized at the mechanistic level as that of synthesis. A wide variety of different enzymes that are capable of splitting peptide bonds are present in cells. However, the bulk of cellular proteolysis seems to be shared between two multienzyme systems: the lysosomal and proteasomal systems. The lysosome is a membrane-enclosed vesicle inside the cell that contains a variety of proteolytic enzymes and operates mostly at acid pH. Volumes of the cytoplasm are engulfed (autophagy) and are then subjected to the action of the protease enzymes at high concentration. This system is thought to be relatively unselective in most cases, although it can also degrade specific intracellular proteins. The system is highly regulated by hormones such as insulin and glucocorticoids, and by amino acids. The second system is the ATP-dependent ubiquitin-proteasome system, which is present in the cytoplasm. The first step is to join molecules of ubiquitin, a basic 76-amino acid peptide, to lysine residues in the target protein. Several enzymes are involved in this process, which selectively targets proteins for degradation by a second component, the proteasome. /Amino acids/
Pharmacodynamics
Insures the adequate absorption of calcium; helps form collagen ( which makes up bone cartilage & connective tissues); aids in the production of antibodies, hormones & enzymes. Recent studies have shown that Lysine may be effective against herpes by improving the balance of nutrients that reduce viral growth. A deficiency may result in tiredness, inability to concentrate, irritability, bloodshot eyes, retarded growth, hair loss, anemia & reproductive problems.
Biological pathways
Source: PubChem (NCBI) · pathways from PathBank, Reactome, WikiPathways & PharmGKB.
This drug in other countries
The same active ingredient registered across other registries we cover - including different brands.