L-Tryptophan
Need Assistance?
  • US & Canada:
    +
  • UK: +

L-Tryptophan

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

L-Tryptophan is an essential amino acid and a precursor to both serotonin and melatonin. Serotonin is a neurotransmitter playing a role in regulating appetite, sleep, mood, and pain. Melatonin is a hormone modulating sleep and wakefulness.
Protein supplement in health care products.

Category
L-Amino Acids
Catalog number
BAT-014312
CAS number
73-22-3
Molecular Formula
C11H12N2O2
Molecular Weight
204.23
L-Tryptophan
IUPAC Name
(2S)-2-amino-3-(1H-indol-3-yl)propanoic acid
Synonyms
H-Trp-OH; L-Tryptophane; L-Tryptohan; Tryptophan, L-; (-)-Tryptophan; (2S)-2-Azaniumyl-3-(1H-indol-3-yl)propanoate; (S)-2-Amino-3-(1H-indol-3-yl)propanoic acid; (S)-Tryptophan; (S)-α-Amino-1H-indole-3-propanoic acid; (S)-α-Amino-β-indolepropionic acid; (S)-α-Aminoindole-3-propionic acid; 1H-Indole-3-alanine, (S)-; 1H-Indole-3-propanoic acid, α-amino-, (S)-; 2-Amino-3-indolylpropanoic acid; 3-Indol-3-ylalanine; L-(-)-Tryptophan; L-Alanine, 3-(1H-indol-3-yl)-; EH 121; l-α-Aminoindole-3-propionic acid; l-β-3-Indolylalanine; Lyphan; NSC 13119; Tryptophan; Tryptophane
Related CAS
6912-86-3 (Deleted CAS) 80206-30-0 (Deleted CAS) 154635-35-5 (Deleted CAS) 2416148-24-6 (Deleted CAS) 2831375-12-1 (Deleted CAS)
Appearance
White to Slightly Yellowish Crystals or Crystalline Powder
Purity
>98%
Density
1.362±0.06 g/cm3
Melting Point
282°C
Boiling Point
447.9±35.0°C at 760 mmHg
Storage
Store at RT
pH
A 1% solution in water has a pH of 5.5 to 7.;
Solubility
Soluble in Water
InChI
InChI=1S/C11H12N2O2/c12-9(11(14)15)5-7-6-13-10-4-2-1-3-8(7)10/h1-4,6,9,13H,5,12H2,(H,14,15)/t9-/m0/s1
InChI Key
QIVBCDIJIAJPQS-VIFPVBQESA-N
Canonical SMILES
C1=CC=C2C(=C1)C(=CN2)CC(C(=O)O)N

L-Tryptophan is an essential amino acid that plays a vital role in a variety of physiological and biochemical processes in the human body. Since the human body cannot synthesize L-Tryptophan, it must be obtained from food sources such as meat, dairy products, nuts, seeds, and legumes. The fundamental importance of L-Tryptophan lies in its involvement in the synthesis of key molecules such as serotonin, melatonin, and niacin, making it key to numerous therapeutic and nutritional interventions. The many applications of L-Tryptophan in health and medicine:

Function in Serotonin Synthesis: One of L-tryptophan's primary uses is in the synthesis of serotonin. One neurotransmitter that significantly affects mood, emotion, and sleep is serotonin. Following consumption of food, L-tryptophan is carried to the brain, where it is changed into 5-hydroxytryptophan (5-HTP) and then serotonin. Sufficient quantities of serotonin are necessary for stable moods and good general health.

Treatment of Mood and Depression: One of L-tryptophan's primary uses is the management of mood disorders, especially depression. L-tryptophan is necessary to keep serotonin levels in the brain at optimal levels since it is a precursor to serotonin. Serotonin's function in controlling mood and emotion has earned it the moniker ""feel-good"" neurotransmitter. Studies reveal that symptoms of anxiety and depression are more common in those with low serotonin levels. L-tryptophan supplements may help patients raise their brain's serotonin levels, which can lessen depression symptoms and encourage happier feelings.

Treatment for Sleep Disorders: L-tryptophan is recognized for its possible advantages in fostering sound sleep habits in addition to its function in mood regulation. The brain uses L-tryptophan to produce serotonin, which can subsequently be further processed to produce melatonin, a hormone that controls sleep-wake cycles. Melatonin's role in promoting relaxation and inducing sleep has earned it the moniker ""sleep hormone."" Increasing the body's supply of L-tryptophan may lead to better sleep patterns and higher-quality sleep for individuals.

Synthesis of Niacin: Another significant chemical made from L-tryptophan is niacin, also known as vitamin B3. The synthesis of energy and cellular metabolism depend on niacin. Although the body is capable of converting L-tryptophan to niacin, this process is not particularly effective; roughly 60 mg of L-tryptophan are needed to generate 1 mg of niacin. But in cases where dietary niacin consumption is inadequate, L-tryptophan can be taken as a supplement to assist avoid pellagra and other disorders like niacin deficient.

Pain Management: Emerging research also suggests the potential of L-tryptophan in pain management. The role of serotonin in regulating pain perception is well established. By enhancing serotonin synthesis, L-tryptophan can help reduce pain perception. Some studies suggest that supplementing with L-tryptophan may benefit conditions such as chronic pain syndromes, fibromyalgia, and migraines.

Immune Function: L-tryptophan is also involved in maintaining a strong immune system. It is a precursor to kynurenine, which plays a role in immune tolerance and regulation. Immune cells metabolize L-tryptophan to regulate T-cell function and defend against pathogens. Therefore, ensuring adequate intake of L-tryptophan can support the immune system and make the body more resistant to infection and disease.

Dietary Supplements and Applications: In dietary supplements, L-tryptophan is available in a variety of forms, including tablets, capsules, and powders. These supplements are often used to treat depression, anxiety, insomnia, and premenstrual dysphoric disorder (PMDD). In clinical settings, L-tryptophan is often used to improve mood, improve sleep quality, and support cognitive and immune function.

1.Assessment of tryptophan metabolism and signs of depression in individuals with carbohydrate malabsorption.
Enko D;Wagner H;Kriegshäuser G;Brandmayr W;Halwachs-Baumann G;Schnedl WJ;Zelzer S;Mangge H;Meinitzer A Psychiatry Res. 2018 Apr;262:595-599. doi: 10.1016/j.psychres.2017.09.049. Epub 2017 Sep 22.
This prospective cross-sectional study aimed to investigate the potential association between primary-adult lactose malabsorption, fructose malabsorption, tryptophan (TRP) metabolism and the presence of depressive signs. Overall 251 patients, who were referred for lactase gene C/T;-13910; polymorphism genotyping and fructose hydrogen/methane breath testing, were included. All participants filled out the Beck Depression Inventory (BDI II). Serum concentrations of tryptophan (TRP), kynurenine (KYN), kynuric acid (KYNA), and TRP competing amino acids (leucine, isoleucine, valine, phenylalanine, tyrosine) were measured by high-pressure liquid-chromatography. Logistic regression analysis was performed with lactose malabsorption, fructose malabsorption and all potential biomarkers of TRP metabolism to assess the effect on signs of depression, defined as a BDI II score > 13. Primary-adult lactose malabsorption and fructose malabsorption was detected in 65 (25.90%) and 65 (25.90%) patients, respectively. Fructose malabsorption was significantly associated with BDI II score, whereas no such relationship was found for lactose malabsorption. Serum levels of TRP and TRP metabolites were no predictors of depression.
2.Short-term supplementation of isocaloric meals with L-tryptophan affects pig growth.
Liu HN;Hu CA;Bai MM;Liu G;Tossou MCB;Xu K;Li FN;Liao P;Kong XF;Wu X;Yin YL Amino Acids. 2017 Dec;49(12):2009-2014. doi: 10.1007/s00726-017-2440-3. Epub 2017 May 24.
L-Tryptophan (Trp) and some of its metabolites regulate the circadian rhythm in mammals. We aimed to investigate the effects of short-term supplementation of Trp in isocaloric meals on growth performance using the parameters of multiple blood biomarkers and free amino acids in growing pigs. A total of 32 Landrace × Yorkshire barrows with a mean body weight of 8.64 (±1.13) kg were randomly assigned to four groups and then fed with various concentrations of Trp diets daily. Our results showed that sequential supplementation of different concentrations of Trp in isocaloric meals decreased the feed:gain (F:G) ratio (P = 0.079) and plasma urea and albumin (P = 0.019), whereas the level of total protein did not. Among the essential and conditionally essential amino acids, the concentrations of histidine, isoleucine, proline, threonine, arginine, and valine in the plasma decreased (P < 0.05), whereas the concentrations of Trp, glycine, serine, and methionine increased (P < 0.01). In addition, concentrations of branched chain amino acids also significantly decreased (P = 0.004), while the rate of conversion of Trp to branched chain amino acids increased (P < 0.001). Taken together, we show that administration of a high concentration of Trp in breakfast with decreasing concentrations of Trp in lunch and dinner positively affected feed utilization and improved feed efficiency, at least in part, through the optimization of amino acid interconversions and nitrogen utilization.
3.Effects of tryptophan-containing peptides on angiotensin-converting enzyme activity and vessel tone ex vivo and in vivo.
Khedr S;Deussen A;Kopaliani I;Zatschler B;Martin M Eur J Nutr. 2018 Apr;57(3):907-915. doi: 10.1007/s00394-016-1374-y. Epub 2017 Jan 19.
PURPOSE: ;Over-activation of the renin-angiotensin axis and worsening of vascular function are critical contributors to the development of hypertension. Therefore, inhibition of angiotensin-converting enzyme (ACE), a key factor of the renin-angiotensin axis, is a first line treatment of hypertension. Besides pharmaceutical ACE inhibitors, some natural peptides have been shown to exert ACE-inhibiting properties with antihypertensive effects and potentially beneficial effects on vascular function. In this study, the ACE-inhibiting potential and effects on vascular function of tryptophan-containing peptides were evaluated.;METHODS: ;The ACE inhibitory action and stability of tryptophan-containing peptides was tested in endothelial cells-a major source of whole body ACE activity. Furthermore, the efficacy of peptides on vascular ACE activity, as well as vessel tone was assessed both ex vivo and in vivo.;RESULTS: ;In human umbilical vein endothelial cells (HUVEC), isoleucine-tryptophan (IW) had the highest ACE inhibitory efficacy, followed by glutamic acid-tryptophan (EW) and tryptophan-leucine (WL). Whereas none of the peptides affected basal vessel tone (rat aorta), angiotensin I-induced vasoconstriction was blocked.
Online Inquiry
Verification code
Inquiry Basket